User talk:Brian Ochoa/Sandbox 1

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Structural Highlights

BRCA1 is an 1,863 amino acid long protein that contains a ring finger motif from position 24 to 64. The ring motif is part of a larger domain spanning the first one hundred amino acid residues, which is required for the formation of its stable structure. This N-terminus domain is of the most highly conserved region of the BRCA1 gene and several cancer-predisposition mutations have been identified in this region. The ring motif is also a C3HC4 zinc-binding motif, named so for the conserved pattern of cysteine and histidines residues that bind the zinc ions. Ultimately, the ring motif of BRCA1 forms a heterodimer with the ring motif of BARD1 to assemble the functional protein complex. The solution structure of this complex shows that long alpha helices border the zinc binding residues in the ring motif. These alpha helices from the ring motif’s of BRCA1 and BARD1 combine to form a four-helix bundle that stabilizes the heterodimer and positions the zinc binding regions next to one another.

Function

Disease

Relevance

Critical Amino Acids

Abbreviations

BCRA1-breast cancer gene 1; BARD-BRCA1 associated ring domain;

Structural highlights

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