1cdz
From Proteopedia
(New page: 200px<br /> <applet load="1cdz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cdz, resolution 3.2Å" /> '''BRCT DOMAIN FROM DNA...) |
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| - | [[Image:1cdz.gif|left|200px]]<br /> | + | [[Image:1cdz.gif|left|200px]]<br /><applet load="1cdz" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1cdz" size=" | + | |
caption="1cdz, resolution 3.2Å" /> | caption="1cdz, resolution 3.2Å" /> | ||
'''BRCT DOMAIN FROM DNA-REPAIR PROTEIN XRCC1'''<br /> | '''BRCT DOMAIN FROM DNA-REPAIR PROTEIN XRCC1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The BRCT domain (BRCA1 C-terminus), first identified in the breast cancer | + | The BRCT domain (BRCA1 C-terminus), first identified in the breast cancer suppressor protein BRCA1, is an evolutionarily conserved protein-protein interaction region of approximately 95 amino acids found in a large number of proteins involved in DNA repair, recombination and cell cycle control. Here we describe the first three-dimensional structure and fold of a BRCT domain determined by X-ray crystallography at 3.2 A resolution. The structure has been obtained from the C-terminal region of the human DNA repair protein XRCC1, and comprises a four-stranded parallel beta-sheet surrounded by three alpha-helices, which form an autonomously folded domain. The compact XRCC1 structure explains the observed sequence homology between different BRCT motifs and provides a framework for modelling other BRCT domains. Furthermore, the established structure of an XRCC1 BRCT homodimer suggests potential protein-protein interaction sites for the complementary BRCT domain in DNA ligase III, since these two domains form a stable heterodimeric complex. Based on the XRCC1 BRCT structure, we have constructed a model for the C-terminal BRCT domain of BRCA1, which frequently is mutated in familial breast and ovarian cancer. The model allows insights into the effects of such mutations on the fold of the BRCT domain. |
==About this Structure== | ==About this Structure== | ||
| - | 1CDZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1CDZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: xrcc1]] | [[Category: xrcc1]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:02 2008'' |
Revision as of 10:05, 21 February 2008
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BRCT DOMAIN FROM DNA-REPAIR PROTEIN XRCC1
Overview
The BRCT domain (BRCA1 C-terminus), first identified in the breast cancer suppressor protein BRCA1, is an evolutionarily conserved protein-protein interaction region of approximately 95 amino acids found in a large number of proteins involved in DNA repair, recombination and cell cycle control. Here we describe the first three-dimensional structure and fold of a BRCT domain determined by X-ray crystallography at 3.2 A resolution. The structure has been obtained from the C-terminal region of the human DNA repair protein XRCC1, and comprises a four-stranded parallel beta-sheet surrounded by three alpha-helices, which form an autonomously folded domain. The compact XRCC1 structure explains the observed sequence homology between different BRCT motifs and provides a framework for modelling other BRCT domains. Furthermore, the established structure of an XRCC1 BRCT homodimer suggests potential protein-protein interaction sites for the complementary BRCT domain in DNA ligase III, since these two domains form a stable heterodimeric complex. Based on the XRCC1 BRCT structure, we have constructed a model for the C-terminal BRCT domain of BRCA1, which frequently is mutated in familial breast and ovarian cancer. The model allows insights into the effects of such mutations on the fold of the BRCT domain.
About this Structure
1CDZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of an XRCC1 BRCT domain: a new protein-protein interaction module., Zhang X, Morera S, Bates PA, Whitehead PC, Coffer AI, Hainbucher K, Nash RA, Sternberg MJ, Lindahl T, Freemont PS, EMBO J. 1998 Nov 2;17(21):6404-11. PMID:9799248
Page seeded by OCA on Thu Feb 21 12:05:02 2008
Categories: Homo sapiens | Single protein | Bates, P. | Coffer, A. | Freemont, P. | Hainbucher, K. | Lindahl, T. | Morera, S. | Nash, R. | Sternberg, M. | Whitehead, P. | Zhang, X. | Brca1 | Brct | Protein-protein interaction | Xrcc1
