3C5R

Crystal Structure of the BARD1 Ankyrin Repeat Domain and Its Functional Consequences

Summary for 3C5R

• Entry DOI: 10.2210/pdb3c5r/pdb
• Descriptor: BRCA1-associated RING domain protein 1 (2 entities in total)
• Functional Keywords: bard1, ankyrin repeat, helix, extended loop, four repeat, protein, ank repeat, disease mutation, metal-binding, nucleus, zinc-finger, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q99728
• Total number of polymer chains: 2
• Total formula weight: 29953.48

Authors

Fox III, D.,Le Trong, I.,Stenkamp, R.E.,Klevit, R.E. (deposition date: 2008-02-01, release date: 2008-05-13, Last modification date: 2023-08-30)

Primary citation

Fox, D.,Le Trong, I.,Rajagopal, P.,Brzovic, P.S.,Stenkamp, R.E.,Klevit, R.E.
Crystal Structure of the BARD1 Ankyrin Repeat Domain and Its Functional Consequences.
J.Biol.Chem., 283:21179-21186, 2008

PubMed Abstract: 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.

PubMed: 18480049
DOI: 10.1074/jbc.M802333200

Experimental method

X-RAY DIFFRACTION (2 Å)