Structure and Interactions of the Human Programmed Cell Death 1 Receptor

PD-1, a receptor expressed by T cells, B cells, and monocytes, is a potent regulator of immune responses and a promising therapeutic target. The structure and interactions of human PD-1 are, however, incompletely characterized. We present the solution nuclear magnetic resonance (NMR)-based structure...

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Published inThe Journal of biological chemistry Vol. 288; no. 17; pp. 11771 - 11785
Main Authors Cheng, Xiaoxiao, Veverka, Vaclav, Radhakrishnan, Anand, Waters, Lorna C., Muskett, Frederick W., Morgan, Sara H., Huo, Jiandong, Yu, Chao, Evans, Edward J., Leslie, Alasdair J., Griffiths, Meryn, Stubberfield, Colin, Griffin, Robert, Henry, Alistair J., Jansson, Andreas, Ladbury, John E., Ikemizu, Shinji, Carr, Mark D., Davis, Simon J.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 26.04.2013
American Society for Biochemistry and Molecular Biology
Subjects
Affinity
Animals
Antigen-Presenting Cells - chemistry
Antigen-Presenting Cells - immunology
Antigen-Presenting Cells - metabolism
B7-1 Antigen - chemistry
B7-1 Antigen - genetics
B7-1 Antigen - immunology
B7-1 Antigen - metabolism
B7-H1 Antigen - chemistry
B7-H1 Antigen - genetics
B7-H1 Antigen - immunology
B7-H1 Antigen - metabolism
Cell Communication - immunology
Cell Surface Protein
Complex Formation
Humans
Immunology
Mice
Models, Immunological
Natural sciences
Naturvetenskap
Nuclear Magnetic Resonance
Nuclear Magnetic Resonance, Biomolecular
Programmed Cell Death 1 Ligand 2 Protein - chemistry
Programmed Cell Death 1 Ligand 2 Protein - genetics
Programmed Cell Death 1 Ligand 2 Protein - immunology
Programmed Cell Death 1 Ligand 2 Protein - metabolism
Programmed Cell Death 1 Receptor - chemistry
Programmed Cell Death 1 Receptor - genetics
Programmed Cell Death 1 Receptor - immunology
Programmed Cell Death 1 Receptor - metabolism
Protein Binding
Protein Structure, Secondary
Receptors
Signaling
Structure-Activity Relationship
Surface Plasmon Resonance
Surface Plasmon Resonance (SPR)
T-Lymphocytes - chemistry
T-Lymphocytes - immunology
T-Lymphocytes - metabolism
Thermodynamics
Nuclear Magnetic Resonance
Signaling
Thermodynamics
Receptors
Surface Plasmon Resonance (SPR)
Cell Surface Protein
Complex Formation
Affinity
Online AccessGet full text

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Abstract PD-1, a receptor expressed by T cells, B cells, and monocytes, is a potent regulator of immune responses and a promising therapeutic target. The structure and interactions of human PD-1 are, however, incompletely characterized. We present the solution nuclear magnetic resonance (NMR)-based structure of the human PD-1 extracellular region and detailed analyses of its interactions with its ligands, PD-L1 and PD-L2. PD-1 has typical immunoglobulin superfamily topology but differs at the edge of the GFCC′ sheet, which is flexible and completely lacks a C″ strand. Changes in PD-1 backbone NMR signals induced by ligand binding suggest that, whereas binding is centered on the GFCC′ sheet, PD-1 is engaged by its two ligands differently and in ways incompletely explained by crystal structures of mouse PD-1·ligand complexes. The affinities of these interactions and that of PD-L1 with the costimulatory protein B7-1, measured using surface plasmon resonance, are significantly weaker than expected. The 3–4-fold greater affinity of PD-L2 versus PD-L1 for human PD-1 is principally due to the 3-fold smaller dissociation rate for PD-L2 binding. Isothermal titration calorimetry revealed that the PD-1/PD-L1 interaction is entropically driven, whereas PD-1/PD-L2 binding has a large enthalpic component. Mathematical simulations based on the biophysical data and quantitative expression data suggest an unexpectedly limited contribution of PD-L2 to PD-1 ligation during interactions of activated T cells with antigen-presenting cells. These findings provide a rigorous structural and biophysical framework for interpreting the important functions of PD-1 and reveal that potent inhibitory signaling can be initiated by weakly interacting receptors. Background: The inhibitory leukocyte receptor PD-1 binds two ligands, PD-L1 and PD-L2. Results: Nuclear magnetic resonance analysis and rigorous binding and thermodynamic measurements reveal the structure of, and the mode of ligand recognition by, PD-1. Conclusion: PD-L1 and PD-L2 bind differently to PD-1 and much more weakly than expected. Significance: Potent inhibitory signaling can be initiated by weakly interacting receptors.
AbstractList Background: The inhibitory leukocyte receptor PD-1 binds two ligands, PD-L1 and PD-L2. Results: Nuclear magnetic resonance analysis and rigorous binding and thermodynamic measurements reveal the structure of, and the mode of ligand recognition by, PD-1. Conclusion: PD-L1 and PD-L2 bind differently to PD-1 and much more weakly than expected. Significance: Potent inhibitory signaling can be initiated by weakly interacting receptors. PD-1, a receptor expressed by T cells, B cells, and monocytes, is a potent regulator of immune responses and a promising therapeutic target. The structure and interactions of human PD-1 are, however, incompletely characterized. We present the solution nuclear magnetic resonance (NMR)-based structure of the human PD-1 extracellular region and detailed analyses of its interactions with its ligands, PD-L1 and PD-L2. PD-1 has typical immunoglobulin superfamily topology but differs at the edge of the GFCC′ sheet, which is flexible and completely lacks a C″ strand. Changes in PD-1 backbone NMR signals induced by ligand binding suggest that, whereas binding is centered on the GFCC′ sheet, PD-1 is engaged by its two ligands differently and in ways incompletely explained by crystal structures of mouse PD-1·ligand complexes. The affinities of these interactions and that of PD-L1 with the costimulatory protein B7-1, measured using surface plasmon resonance, are significantly weaker than expected. The 3–4-fold greater affinity of PD-L2 versus PD-L1 for human PD-1 is principally due to the 3-fold smaller dissociation rate for PD-L2 binding. Isothermal titration calorimetry revealed that the PD-1/PD-L1 interaction is entropically driven, whereas PD-1/PD-L2 binding has a large enthalpic component. Mathematical simulations based on the biophysical data and quantitative expression data suggest an unexpectedly limited contribution of PD-L2 to PD-1 ligation during interactions of activated T cells with antigen-presenting cells. These findings provide a rigorous structural and biophysical framework for interpreting the important functions of PD-1 and reveal that potent inhibitory signaling can be initiated by weakly interacting receptors.
PD-1, a receptor expressed by T cells, B cells, and monocytes, is a potent regulator of immune responses and a promising therapeutic target. The structure and interactions of human PD-1 are, however, incompletely characterized. We present the solution nuclear magnetic resonance (NMR)-based structure of the human PD-1 extracellular region and detailed analyses of its interactions with its ligands, PD-L1 and PD-L2. PD-1 has typical immunoglobulin superfamily topology but differs at the edge of the GFCC' sheet, which is flexible and completely lacks a C" strand. Changes in PD-1 backbone NMR signals induced by ligand binding suggest that, whereas binding is centered on the GFCC' sheet, PD-1 is engaged by its two ligands differently and in ways incompletely explained by crystal structures of mouse PD-1 · ligand complexes. The affinities of these interactions and that of PD-L1 with the costimulatory protein B7-1, measured using surface plasmon resonance, are significantly weaker than expected. The 3-4-fold greater affinity of PD-L2 versus PD-L1 for human PD-1 is principally due to the 3-fold smaller dissociation rate for PD-L2 binding. Isothermal titration calorimetry revealed that the PD-1/PD-L1 interaction is entropically driven, whereas PD-1/PD-L2 binding has a large enthalpic component. Mathematical simulations based on the biophysical data and quantitative expression data suggest an unexpectedly limited contribution of PD-L2 to PD-1 ligation during interactions of activated T cells with antigen-presenting cells. These findings provide a rigorous structural and biophysical framework for interpreting the important functions of PD-1 and reveal that potent inhibitory signaling can be initiated by weakly interacting receptors.
PD-1, a receptor expressed by T cells, B cells, and monocytes, is a potent regulator of immune responses and a promising therapeutic target. The structure and interactions of human PD-1 are, however, incompletely characterized. We present the solution nuclear magnetic resonance (NMR)-based structure of the human PD-1 extracellular region and detailed analyses of its interactions with its ligands, PD-L1 and PD-L2. PD-1 has typical immunoglobulin superfamily topology but differs at the edge of the GFCC' sheet, which is flexible and completely lacks a C '' strand. Changes in PD-1 backbone NMR signals induced by ligand binding suggest that, whereas binding is centered on the GFCC' sheet, PD-1 is engaged by its two ligands differently and in ways incompletely explained by crystal structures of mouse PD-1.ligand complexes. The affinities of these interactions and that of PD-L1 with the costimulatory protein B7-1, measured using surface plasmon resonance, are significantly weaker than expected. The 3-4-fold greater affinity of PD-L2 versus PD-L1 for human PD-1 is principally due to the 3-fold smaller dissociation rate for PD-L2 binding. Isothermal titration calorimetry revealed that the PD-1/PD-L1 interaction is entropically driven, whereas PD-1/PD-L2 binding has a large enthalpic component. Mathematical simulations based on the biophysical data and quantitative expression data suggest an unexpectedly limited contribution of PD-L2 to PD-1 ligation during interactions of activated T cells with antigen-presenting cells. These findings provide a rigorous structural and biophysical framework for interpreting the important functions of PD-1 and reveal that potent inhibitory signaling can be initiated by weakly interacting receptors.
PD-1, a receptor expressed by T cells, B cells, and monocytes, is a potent regulator of immune responses and a promising therapeutic target. The structure and interactions of human PD-1 are, however, incompletely characterized. We present the solution nuclear magnetic resonance (NMR)-based structure of the human PD-1 extracellular region and detailed analyses of its interactions with its ligands, PD-L1 and PD-L2. PD-1 has typical immunoglobulin superfamily topology but differs at the edge of the GFCC′ sheet, which is flexible and completely lacks a C″ strand. Changes in PD-1 backbone NMR signals induced by ligand binding suggest that, whereas binding is centered on the GFCC′ sheet, PD-1 is engaged by its two ligands differently and in ways incompletely explained by crystal structures of mouse PD-1·ligand complexes. The affinities of these interactions and that of PD-L1 with the costimulatory protein B7-1, measured using surface plasmon resonance, are significantly weaker than expected. The 3–4-fold greater affinity of PD-L2 versus PD-L1 for human PD-1 is principally due to the 3-fold smaller dissociation rate for PD-L2 binding. Isothermal titration calorimetry revealed that the PD-1/PD-L1 interaction is entropically driven, whereas PD-1/PD-L2 binding has a large enthalpic component. Mathematical simulations based on the biophysical data and quantitative expression data suggest an unexpectedly limited contribution of PD-L2 to PD-1 ligation during interactions of activated T cells with antigen-presenting cells. These findings provide a rigorous structural and biophysical framework for interpreting the important functions of PD-1 and reveal that potent inhibitory signaling can be initiated by weakly interacting receptors. Background: The inhibitory leukocyte receptor PD-1 binds two ligands, PD-L1 and PD-L2. Results: Nuclear magnetic resonance analysis and rigorous binding and thermodynamic measurements reveal the structure of, and the mode of ligand recognition by, PD-1. Conclusion: PD-L1 and PD-L2 bind differently to PD-1 and much more weakly than expected. Significance: Potent inhibitory signaling can be initiated by weakly interacting receptors.
Author Cheng, Xiaoxiao
Waters, Lorna C.
Muskett, Frederick W.
Griffin, Robert
Stubberfield, Colin
Griffiths, Meryn
Ladbury, John E.
Carr, Mark D.
Morgan, Sara H.
Radhakrishnan, Anand
Veverka, Vaclav
Huo, Jiandong
Ikemizu, Shinji
Jansson, Andreas
Leslie, Alasdair J.
Yu, Chao
Henry, Alistair J.
Evans, Edward J.
Davis, Simon J.
Author_xml – sequence: 1
  givenname: Xiaoxiao
  surname: Cheng
  fullname: Cheng, Xiaoxiao
  organization: Radcliffe Department of Medicine, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DU, United Kingdom
– sequence: 2
  givenname: Vaclav
  surname: Veverka
  fullname: Veverka, Vaclav
  organization: Department of Biochemistry, University of Leicester, Leicester LE1 9HN, United Kingdom
– sequence: 3
  givenname: Anand
  surname: Radhakrishnan
  fullname: Radhakrishnan, Anand
  organization: Department of Biochemistry and Molecular Biology, University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030
– sequence: 4
  givenname: Lorna C.
  surname: Waters
  fullname: Waters, Lorna C.
  organization: Department of Biochemistry, University of Leicester, Leicester LE1 9HN, United Kingdom
– sequence: 5
  givenname: Frederick W.
  surname: Muskett
  fullname: Muskett, Frederick W.
  organization: Department of Biochemistry, University of Leicester, Leicester LE1 9HN, United Kingdom
– sequence: 6
  givenname: Sara H.
  surname: Morgan
  fullname: Morgan, Sara H.
  organization: Radcliffe Department of Medicine, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DU, United Kingdom
– sequence: 7
  givenname: Jiandong
  surname: Huo
  fullname: Huo, Jiandong
  organization: Radcliffe Department of Medicine, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DU, United Kingdom
– sequence: 8
  givenname: Chao
  surname: Yu
  fullname: Yu, Chao
  organization: Radcliffe Department of Medicine, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DU, United Kingdom
– sequence: 9
  givenname: Edward J.
  surname: Evans
  fullname: Evans, Edward J.
  organization: Radcliffe Department of Medicine, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DU, United Kingdom
– sequence: 10
  givenname: Alasdair J.
  surname: Leslie
  fullname: Leslie, Alasdair J.
  organization: Radcliffe Department of Medicine, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DU, United Kingdom
– sequence: 11
  givenname: Meryn
  surname: Griffiths
  fullname: Griffiths, Meryn
  organization: UCB Pharma, Slough SL1 4EN, United Kingdom
– sequence: 12
  givenname: Colin
  surname: Stubberfield
  fullname: Stubberfield, Colin
  organization: UCB Pharma, Slough SL1 4EN, United Kingdom
– sequence: 13
  givenname: Robert
  surname: Griffin
  fullname: Griffin, Robert
  organization: UCB Pharma, Slough SL1 4EN, United Kingdom
– sequence: 14
  givenname: Alistair J.
  surname: Henry
  fullname: Henry, Alistair J.
  organization: UCB Pharma, Slough SL1 4EN, United Kingdom
– sequence: 15
  givenname: Andreas
  surname: Jansson
  fullname: Jansson, Andreas
  organization: Systems Biology Research Centre, School of Life Sciences, University of Skövde, Box 408, Skövde, Sweden
– sequence: 16
  givenname: John E.
  surname: Ladbury
  fullname: Ladbury, John E.
  organization: Systems Biology Research Centre, School of Life Sciences, University of Skövde, Box 408, Skövde, Sweden
– sequence: 17
  givenname: Shinji
  surname: Ikemizu
  fullname: Ikemizu, Shinji
  organization: Division of Structural Biology, Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-honmachi, Kumamoto 862 0973, Japan
– sequence: 18
  givenname: Mark D.
  surname: Carr
  fullname: Carr, Mark D.
  email: mdc12@le.ac.uk
  organization: Department of Biochemistry, University of Leicester, Leicester LE1 9HN, United Kingdom
– sequence: 19
  givenname: Simon J.
  surname: Davis
  fullname: Davis, Simon J.
  email: simon.davis@imm.ox.ac.uk
  organization: Radcliffe Department of Medicine, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DU, United Kingdom
BackLink https://www.ncbi.nlm.nih.gov/pubmed/23417675$$D View this record in MEDLINE/PubMed
https://urn.kb.se/resolve?urn=urn:nbn:se:his:diva-8400$$DView record from Swedish Publication Index
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Issue 17
Keywords Nuclear Magnetic Resonance
Signaling
Thermodynamics
Receptors
Surface Plasmon Resonance (SPR)
Cell Surface Protein
Complex Formation
Affinity
Language English
License This is an open access article under the CC BY license.
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Snippet PD-1, a receptor expressed by T cells, B cells, and monocytes, is a potent regulator of immune responses and a promising therapeutic target. The structure and...
Background: The inhibitory leukocyte receptor PD-1 binds two ligands, PD-L1 and PD-L2. Results: Nuclear magnetic resonance analysis and rigorous binding and...
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proquest
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StartPage 11771
SubjectTerms Affinity
Animals
Antigen-Presenting Cells - chemistry
Antigen-Presenting Cells - immunology
Antigen-Presenting Cells - metabolism
B7-1 Antigen - chemistry
B7-1 Antigen - genetics
B7-1 Antigen - immunology
B7-1 Antigen - metabolism
B7-H1 Antigen - chemistry
B7-H1 Antigen - genetics
B7-H1 Antigen - immunology
B7-H1 Antigen - metabolism
Cell Communication - immunology
Cell Surface Protein
Complex Formation
Humans
Immunology
Mice
Models, Immunological
Natural sciences
Naturvetenskap
Nuclear Magnetic Resonance
Nuclear Magnetic Resonance, Biomolecular
Programmed Cell Death 1 Ligand 2 Protein - chemistry
Programmed Cell Death 1 Ligand 2 Protein - genetics
Programmed Cell Death 1 Ligand 2 Protein - immunology
Programmed Cell Death 1 Ligand 2 Protein - metabolism
Programmed Cell Death 1 Receptor - chemistry
Programmed Cell Death 1 Receptor - genetics
Programmed Cell Death 1 Receptor - immunology
Programmed Cell Death 1 Receptor - metabolism
Protein Binding
Protein Structure, Secondary
Receptors
Signaling
Structure-Activity Relationship
Surface Plasmon Resonance
Surface Plasmon Resonance (SPR)
T-Lymphocytes - chemistry
T-Lymphocytes - immunology
T-Lymphocytes - metabolism
Thermodynamics
Title Structure and Interactions of the Human Programmed Cell Death 1 Receptor
URI https://dx.doi.org/10.1074/jbc.M112.448126
https://www.ncbi.nlm.nih.gov/pubmed/23417675
https://search.proquest.com/docview/1347257505
https://pubmed.ncbi.nlm.nih.gov/PMC3636866
https://urn.kb.se/resolve?urn=urn:nbn:se:his:diva-8400
Volume 288
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