1gxc: Difference between revisions

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[[Image:1gxc.~~gif~~|left|200px]]

[[Image:1gxc.png|left|200px]]

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

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

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_12049740}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12049740 is the PubMed ID number.

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==About this Structure==

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[[Category: Serine/threonine-protein kinase]]

[[Category: Transferase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 18~~:08:17 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:16:05 2008''

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-[[Image:1gxc.gif|left|200px]]
+{{Seed}}
+[[Image:1gxc.png|left|200px]]
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 {{STRUCTURE_1gxc|  PDB=1gxc  |  SCENE=  }}
-'''FHA DOMAIN FROM HUMAN CHK2 KINASE IN COMPLEX WITH A SYNTHETIC PHOSPHOPEPTIDE'''
+===FHA DOMAIN FROM HUMAN CHK2 KINASE IN COMPLEX WITH A SYNTHETIC PHOSPHOPEPTIDE===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12049740}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12049740 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12049740}}
 ==About this Structure==
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 [[Category: Serine/threonine-protein kinase]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:08:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 06:16:05 2008''