Structural characterization of BRCT–tetrapeptide binding interactions
BRCT(BRCA1) plays a major role in DNA repair pathway, and does so by recognizing the conserved sequence pSXXF in its target proteins. Remarkably, tetrapeptides containing pSXXF motif bind with high specificity and micromolar affinity. Here, we have characterized the binding interactions of pSXXF tet...
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| Published in | Biochemical and biophysical research communications Vol. 393; no. 2; pp. 207 - 210 |
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| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
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Elsevier Inc
05.03.2010
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| Abstract | BRCT(BRCA1) plays a major role in DNA repair pathway, and does so by recognizing the conserved sequence pSXXF in its target proteins. Remarkably, tetrapeptides containing pSXXF motif bind with high specificity and micromolar affinity. Here, we have characterized the binding interactions of pSXXF tetrapeptides using NMR spectroscopy and calorimetry. We show that BRCT is dynamic and becomes structured on binding, that pSer and Phe residues dictate overall binding, and that the binding affinities of the tetrapeptides are intimately linked to structural and dynamic changes both in the BRCT(BRCA1) and tetrapeptides. These results provide critical insights for designing high-affinity BRCT(BRCA1) inhibitors. |
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| AbstractList | BRCT(BRCA1) plays a major role in DNA repair pathway, and does so by recognizing the conserved sequence pSXXF in its target proteins. Remarkably, tetrapeptides containing pSXXF motif bind with high specificity and micromolar affinity. Here, we have characterized the binding interactions of pSXXF tetrapeptides using NMR spectroscopy and calorimetry. We show that BRCT is dynamic and becomes structured on binding, that pSer and Phe residues dictate overall binding, and that the binding affinities of the tetrapeptides are intimately linked to structural and dynamic changes both in the BRCT(BRCA1) and tetrapeptides. These results provide critical insights for designing high-affinity BRCT(BRCA1) inhibitors. |
| Author | Kumar, Eric A. Natarajan, Amarnath Joseph, Prem Raj B. Kizhake, Smitha Rajarathnam, Krishna Lokesh, G.L. Yuan, Ziyan |
| AuthorAffiliation | Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555 Eppley Institute for Cancer Research, University of Nebraska Medical Center, Omaha, NE 68198 ξ Sealy Center for Cancer Cell Biology, University of Texas Medical Branch, Galveston, TX 77555 χ Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555 Chemical Biology Program, Department of Pharmacology and Toxicology, University of Texas Medical Branch, Galveston, TX 77555 |
| AuthorAffiliation_xml | – name: Eppley Institute for Cancer Research, University of Nebraska Medical Center, Omaha, NE 68198 – name: Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555 – name: χ Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555 – name: ξ Sealy Center for Cancer Cell Biology, University of Texas Medical Branch, Galveston, TX 77555 – name: Chemical Biology Program, Department of Pharmacology and Toxicology, University of Texas Medical Branch, Galveston, TX 77555 |
| Author_xml | – sequence: 1 givenname: Prem Raj B. surname: Joseph fullname: Joseph, Prem Raj B. organization: Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, USA – sequence: 2 givenname: Ziyan surname: Yuan fullname: Yuan, Ziyan organization: Chemical Biology Program, Department of Pharmacology and Toxicology, University of Texas Medical Branch, Galveston, TX 77555, USA – sequence: 3 givenname: Eric A. surname: Kumar fullname: Kumar, Eric A. organization: Chemical Biology Program, Department of Pharmacology and Toxicology, University of Texas Medical Branch, Galveston, TX 77555, USA – sequence: 4 givenname: G.L. surname: Lokesh fullname: Lokesh, G.L. organization: Chemical Biology Program, Department of Pharmacology and Toxicology, University of Texas Medical Branch, Galveston, TX 77555, USA – sequence: 5 givenname: Smitha surname: Kizhake fullname: Kizhake, Smitha organization: Chemical Biology Program, Department of Pharmacology and Toxicology, University of Texas Medical Branch, Galveston, TX 77555, USA – sequence: 6 givenname: Krishna surname: Rajarathnam fullname: Rajarathnam, Krishna email: krrajara@utmb.edu organization: Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, USA – sequence: 7 givenname: Amarnath surname: Natarajan fullname: Natarajan, Amarnath email: anatarajan@unmc.edu organization: Chemical Biology Program, Department of Pharmacology and Toxicology, University of Texas Medical Branch, Galveston, TX 77555, USA |
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| Cites_doi | 10.1021/ja0739178 10.1021/ja982649y 10.1126/science.1088753 10.1038/nsmb775 10.1128/MCB.24.21.9478-9486.2004 10.1038/nsmb776 10.1126/science.1139476 10.1016/j.str.2004.06.002 10.1016/S1097-2765(04)00238-2 10.1126/science.1088877 10.1016/S0092-8674(01)00304-X 10.1021/bi901194p 10.1126/science.7939630 10.1016/S0955-0674(03)00042-5 10.1021/bi800314m 10.1021/bi0509651 |
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| Keywords | pSXXF tetrapeptide Thermodynamics TROSY NMR BRCT(BRCA1) ITC Structure |
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| Snippet | BRCT(BRCA1) plays a major role in DNA repair pathway, and does so by recognizing the conserved sequence pSXXF in its target proteins. Remarkably, tetrapeptides... |
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| SubjectTerms | Amino Acid Motifs BRCA1 Protein - antagonists & inhibitors BRCA1 Protein - chemistry BRCT(BRCA1) Drug Design Humans NMR Nuclear Magnetic Resonance, Biomolecular Oligopeptides - chemistry Protein Binding Protein Conformation pSXXF tetrapeptide Structure Thermodynamics |
| Title | Structural characterization of BRCT–tetrapeptide binding interactions |
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