1t29: Difference between revisions

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[[Image:1t29.gif|left|200px]]
{{Seed}}
[[Image:1t29.png|left|200px]]


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{{STRUCTURE_1t29|  PDB=1t29  |  SCENE=  }}  
{{STRUCTURE_1t29|  PDB=1t29  |  SCENE=  }}  


'''Crystal structure of the BRCA1 BRCT repeats bound to a phosphorylated BACH1 peptide'''
===Crystal structure of the BRCA1 BRCT repeats bound to a phosphorylated BACH1 peptide===




==Overview==
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The recognition of the phosphorylated BACH1 helicase by the BRCA1 C-terminal (BRCT) repeats is important to the tumor suppressor function of BRCA1. Here we report the crystal structure of the BRCT repeats of human BRCA1 bound to a phosphorylated BACH1 peptide at 2.3 A resolution. The phosphorylated serine 990 and phenylalanine 993 of BACH1 anchor the binding to BRCA1 through specific interactions with a surface cleft at the junction of the two BRCT repeats. This surface cleft is highly conserved in BRCA1 across species, suggesting an evolutionarily conserved function of phosphopeptide recognition. Importantly, conserved amino acids critical for BACH1 binding are frequently targeted for missense mutations in breast cancer. These mutations greatly diminish the ability of BRCA1 to interact with the phosphorylated BACH1 peptide. Additional structural analysis revealed significant implications for understanding the function of the BRCT family of proteins in DNA damage and repair signaling.
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{{ABSTRACT_PUBMED_15125843}}


==About this Structure==
==About this Structure==
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[[Category: Breast cancer]]
[[Category: Breast cancer]]
[[Category: Phosphopeptide recognition]]
[[Category: Phosphopeptide recognition]]
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Revision as of 04:03, 29 July 2008

File:1t29.png

Template:STRUCTURE 1t29

Crystal structure of the BRCA1 BRCT repeats bound to a phosphorylated BACH1 peptide

Template:ABSTRACT PUBMED 15125843

About this Structure

1T29 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling., Shiozaki EN, Gu L, Yan N, Shi Y, Mol Cell. 2004 May 7;14(3):405-12. PMID:15125843

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