1gxc

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{{STRUCTURE_1gxc| PDB=1gxc | SCENE= }}
{{STRUCTURE_1gxc| PDB=1gxc | SCENE= }}
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'''FHA DOMAIN FROM HUMAN CHK2 KINASE IN COMPLEX WITH A SYNTHETIC PHOSPHOPEPTIDE'''
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===FHA DOMAIN FROM HUMAN CHK2 KINASE IN COMPLEX WITH A SYNTHETIC PHOSPHOPEPTIDE===
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==Overview==
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The Chk2 Ser/Thr kinase plays crucial, evolutionarily conserved roles in cellular responses to DNA damage. Identification of two pro-oncogenic mutations within the Chk2 FHA domain has highlighted its importance for Chk2 function in checkpoint activation. The X-ray structure of the Chk2 FHA domain in complex with an in vitro selected phosphopeptide motif reveals the determinants of binding specificity and shows that both mutations are remote from the peptide binding site. We show that the Chk2 FHA domain mediates ATM-dependent Chk2 phosphorylation and targeting of Chk2 to in vivo binding partners such as BRCA1 through either or both of two structurally distinct mechanisms. Although phospho-dependent binding is important for Chk2 activity, previously uncharacterized phospho-independent FHA domain interactions appear to be the primary target of oncogenic lesions.
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{{ABSTRACT_PUBMED_12049740}}
==About this Structure==
==About this Structure==
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[[Category: Serine/threonine-protein kinase]]
[[Category: Serine/threonine-protein kinase]]
[[Category: Transferase]]
[[Category: Transferase]]
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Revision as of 03:16, 1 July 2008

Image:1gxc.png

Template:STRUCTURE 1gxc

FHA DOMAIN FROM HUMAN CHK2 KINASE IN COMPLEX WITH A SYNTHETIC PHOSPHOPEPTIDE

Template:ABSTRACT PUBMED 12049740

About this Structure

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

Reference

Structural and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2., Li J, Williams BL, Haire LF, Goldberg M, Wilker E, Durocher D, Yaffe MB, Jackson SP, Smerdon SJ, Mol Cell. 2002 May;9(5):1045-54. PMID:12049740

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