The Crystal Structure of the Chemokine Domain of Fractalkine Shows a Novel Quaternary Arrangement

Fractalkine, or neurotactin, is a chemokine that is present in endothelial cells from several tissues, including brain, liver, and kidney. It is the only member of the CX3C class of chemokines. Fractalkine contains a chemokine domain (CDF) attached to a membrane-spanning domain via a mucin-like stal...

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Published inThe Journal of biological chemistry Vol. 275; no. 30; pp. 23187 - 23193
Main Authors Hoover, David M., Mizoue, Laura S., Handel, Tracy M., Lubkowski, Jacek
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 28.07.2000
American Society for Biochemistry and Molecular Biology
Subjects
Chemokine CX3CL1
Chemokines, CX3C
Chemokines, CXC - chemistry
Crystallography, X-Ray
fractalkine
Membrane Proteins - chemistry
Models, Molecular
Protein Structure, Quaternary
Online AccessGet full text

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Abstract Fractalkine, or neurotactin, is a chemokine that is present in endothelial cells from several tissues, including brain, liver, and kidney. It is the only member of the CX3C class of chemokines. Fractalkine contains a chemokine domain (CDF) attached to a membrane-spanning domain via a mucin-like stalk. However, fractalkine can also be proteolytically cleaved from its membrane-spanning domain to release a freely diffusible form. Fractalkine attracts and immobilizes leukocytes by binding to its receptor, CX3CR1. The x-ray crystal structure of CDF has been solved and refined to 2.0 Å resolution. The CDF monomers form a dimer through an intermolecular β-sheet. This interaction is somewhat similar to that seen in other dimeric CC chemokine crystal structures. However, the displacement of the first disulfide in CDF causes the dimer to assume a more compact quaternary structure relative to CC chemokines, which is unique to CX3C chemokines. Although fractalkine can bind to heparin in vitro, as shown by comparison of electrostatic surface plots with other chemokines and by heparin chromatography, the role of this property in vivois not well understood.
AbstractList Fractalkine, or neurotactin, is a chemokine that is present in endothelial cells from several tissues, including brain, liver, and kidney. It is the only member of the CX3C class of chemokines. Fractalkine contains a chemokine domain (CDF) attached to a membrane-spanning domain via a mucin-like stalk. However, fractalkine can also be proteolytically cleaved from its membrane-spanning domain to release a freely diffusible form. Fractalkine attracts and immobilizes leukocytes by binding to its receptor, CX3CR1. The x-ray crystal structure of CDF has been solved and refined to 2.0 Å resolution. The CDF monomers form a dimer through an intermolecular β-sheet. This interaction is somewhat similar to that seen in other dimeric CC chemokine crystal structures. However, the displacement of the first disulfide in CDF causes the dimer to assume a more compact quaternary structure relative to CC chemokines, which is unique to CX3C chemokines. Although fractalkine can bind to heparin in vitro, as shown by comparison of electrostatic surface plots with other chemokines and by heparin chromatography, the role of this property in vivois not well understood.
Fractalkine, or neurotactin, is a chemokine that is present in endothelial cells from several tissues, including brain, liver, and kidney. It is the only member of the CX(3)C class of chemokines. Fractalkine contains a chemokine domain (CDF) attached to a membrane-spanning domain via a mucin-like stalk. However, fractalkine can also be proteolytically cleaved from its membrane-spanning domain to release a freely diffusible form. Fractalkine attracts and immobilizes leukocytes by binding to its receptor, CX(3)CR1. The x-ray crystal structure of CDF has been solved and refined to 2.0 A resolution. The CDF monomers form a dimer through an intermolecular beta-sheet. This interaction is somewhat similar to that seen in other dimeric CC chemokine crystal structures. However, the displacement of the first disulfide in CDF causes the dimer to assume a more compact quaternary structure relative to CC chemokines, which is unique to CX(3)C chemokines. Although fractalkine can bind to heparin in vitro, as shown by comparison of electrostatic surface plots with other chemokines and by heparin chromatography, the role of this property in vivo is not well understood.
Fractalkine, or neurotactin, is a chemokine that is present in endothelial cells from several tissues, including brain, liver, and kidney. It is the only member of the CX sub(3)C class of chemokines. Fractalkine contains a chemokine domain (CDF) attached to a membrane-spanning domain via a mucin-like stalk. However, fractalkine can also be proteolytically cleaved from its membrane-spanning domain to release a freely diffusible form. Fractalkine attracts and immobilizes leukocytes by binding to its receptor, CX sub(3)CR1. The x-ray crystal structure of CDF has been solved and refined to 2.0 Aa resolution. The CDF monomers form a dimer through an intermolecular beta -sheet. This interaction is somewhat similar to that seen in other dimeric CC chemokine crystal structures. However, the displacement of the first disulfide in CDF causes the dimer to assume a more compact quaternary structure relative to CC chemokines, which is unique to CX sub(3)C chemokines. Although fractalkine can bind to heparin in vitro, as shown by comparison of electrostatic surface plots with other chemokines and by heparin chromatography, the role of this property in vivo is not well understood.
Fractalkine, or neurotactin, is a chemokine that is present in endothelial cells from several tissues, including brain, liver, and kidney. It is the only member of the CX 3 C class of chemokines. Fractalkine contains a chemokine domain (CDF) attached to a membrane-spanning domain via a mucin-like stalk. However, fractalkine can also be proteolytically cleaved from its membrane-spanning domain to release a freely diffusible form. Fractalkine attracts and immobilizes leukocytes by binding to its receptor, CX 3 CR1. The x-ray crystal structure of CDF has been solved and refined to 2.0 Å resolution. The CDF monomers form a dimer through an intermolecular β-sheet. This interaction is somewhat similar to that seen in other dimeric CC chemokine crystal structures. However, the displacement of the first disulfide in CDF causes the dimer to assume a more compact quaternary structure relative to CC chemokines, which is unique to CX 3 C chemokines. Although fractalkine can bind to heparin in vitro , as shown by comparison of electrostatic surface plots with other chemokines and by heparin chromatography, the role of this property in vivo is not well understood.
Author Lubkowski, Jacek
Mizoue, Laura S.
Hoover, David M.
Handel, Tracy M.
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Snippet Fractalkine, or neurotactin, is a chemokine that is present in endothelial cells from several tissues, including brain, liver, and kidney. It is the only...
Fractalkine, or neurotactin, is a chemokine that is present in endothelial cells from several tissues, including brain, liver, and kidney. It is the only...
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StartPage 23187
SubjectTerms Chemokine CX3CL1
Chemokines, CX3C
Chemokines, CXC - chemistry
Crystallography, X-Ray
fractalkine
Membrane Proteins - chemistry
Models, Molecular
Protein Structure, Quaternary
Title The Crystal Structure of the Chemokine Domain of Fractalkine Shows a Novel Quaternary Arrangement
URI https://dx.doi.org/10.1074/jbc.M002584200
http://www.jbc.org/content/275/30/23187.abstract
https://www.ncbi.nlm.nih.gov/pubmed/10770945
https://search.proquest.com/docview/17569989
https://search.proquest.com/docview/71762742
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