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3c5r
From Proteopedia
Contents |
Crystal Structure of the BARD1 Ankyrin Repeat Domain and Its Functional Consequences
BARD1 is the constitutive nuclear partner to the breast and ovarian cancer-specific tumor suppressor BRCA1. Together, they form a heterodimeric complex responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. We report the 2.0A structure of the BARD1 ankyrin repeat domain. The structure includes four ankyrin repeats with a non-canonical C-terminal capping ankyrin repeat and a well ordered extended loop preceding the first repeat. Conserved surface features show an acidic patch and an acidic pocket along the surface typically used by ankyrin repeat domains for binding cognate proteins. We also demonstrate that two reported mutations, N470S and V507M, in the ankyrin repeat domain do not result in observable structural defects. These results provide a structural basis for exploring the biological function of the ankyrin repeat domain and for modeling BARD1 isoforms.
Crystal Structure of the BARD1 Ankyrin Repeat Domain and Its Functional Consequences., Fox D 3rd, Le Trong I, Rajagopal P, Brzovic PS, Stenkamp RE, Klevit RE, J Biol Chem. 2008 Jul 25;283(30):21179-86. Epub 2008 May 14. PMID:18480049
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
Disease
Known disease associated with this structure: Breast cancer, susceptibility to OMIM:[601593]
About this Structure
3C5R is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Fox D 3rd, Le Trong I, Rajagopal P, Brzovic PS, Stenkamp RE, Klevit RE. Crystal structure of the BARD1 ankyrin repeat domain and its functional consequences. J Biol Chem. 2008 Jul 25;283(30):21179-86. Epub 2008 May 14. PMID:18480049 doi:10.1074/jbc.M802333200
Page seeded by OCA on Tue Feb 17 20:32:19 2009
Categories: Homo sapiens | III, D Fox. | Klevit, R E. | Stenkamp, R E. | Trong, I Le. | Ank repeat | Ankyrin repeat | Bard1 | Disease mutation | Extended loop | Four repeat | Helix | Metal-binding | Nucleus | Polymorphism | Protein | Protein binding | Ubl conjugation | Zinc | Zinc-finger
