1oqa: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= BRCA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= BRCA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1jnx|1JNX]], [[1kzy|1KZY]], [[1cdz|1CDZ]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oqa OCA], [http://www.ebi.ac.uk/pdbsum/1oqa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oqa RCSB]</span> | |||
}} | }} | ||
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==Disease== | ==Disease== | ||
Known | Known disease associated with this structure: Breast cancer-1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=113705 113705]], Breast-ovarian cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=113705 113705]], Ovarian cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=113705 113705]], Papillary serous carcinoma of the peritoneum OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=113705 113705]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: breast cancer]] | [[Category: breast cancer]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:48:47 2008'' | ||
Revision as of 22:48, 30 March 2008
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| Gene: | BRCA1 (Homo sapiens) | ||||||
| Related: | 1JNX, 1KZY, 1CDZ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of the BRCT-c domain from human BRCA1
OverviewOverview
BRCA1 is a tumor suppressor protein associated with breast and ovarian cancer. The C-terminal region of BRCA1 consists of two closely spaced BRCT domains which mediate essential biological functions, including regulation of transcription and control of cell-cycle progression by their interaction with phosphorylated effector proteins. Here we report the NMR structure of the isolated C-terminal BRCT domain (BRCT-c) from human BRCA1. BRCT-c is well-structured in solution, folding independently in the absence of its BRCT-n counterpart. Ultracentrifugation experiments and size exclusion chromatography reveal that BRCT-c exists as a monomer under near-physiological conditions. Dynamics measurements from NMR data show three loops which coincide with the most variable sequence regions in BRCT domains, to be genuinely flexible in solution. The solution structure of BRCT-c shows subtle conformational changes when compared to the crystal structure of BRCT-c in the tandem repeat of BRCA1. These affect sites involved in formation of the BRCT-n-BRCT-c interface and the binding to phosphoserine-containing peptides. The results suggest that the presence of native BRCT-n and a properly aligned BRCT-n-BRCT-c interface are essential if BRCT-c is to adopt a biologically active conformation. Structural consequences of cancer-associated mutations and biological implications of the dynamic behavior are discussed.
DiseaseDisease
Known disease associated with this structure: Breast cancer-1 OMIM:[113705], Breast-ovarian cancer OMIM:[113705], Ovarian cancer OMIM:[113705], Papillary serous carcinoma of the peritoneum OMIM:[113705]
About this StructureAbout this Structure
1OQA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure, backbone dynamics, and association behavior of the C-terminal BRCT domain from the breast cancer-associated protein BRCA1., Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kuhne R, Oschkinat H, Heinemann U, Biochemistry. 2004 Dec 28;43(51):15983-95. PMID:15609993
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