1t2v: Difference between revisions

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[[Image:1t2v.~~gif~~|left|200px]]

[[Image:1t2v.png|left|200px]]

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~~'''~~Structural basis of phospho-peptide recognition by the BRCT domain of BRCA1, structure with phosphopeptide~~'''~~

===Structural basis of phospho-peptide recognition by the BRCT domain of BRCA1, structure with phosphopeptide===

~~==Overview==~~

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The ~~BRCT repeats in BRCA1 are essential for its tumor suppressor activity and interact with phosphorylated protein targets containing the sequence pSer-X-X-Phe~~, ~~where X indicates any residue. The structure of~~ the ~~tandem BRCA1 BRCT repeats bound~~ to ~~an optimized phosphopeptide reveals that~~ the ~~N-terminal repeat harbors a conserved BRCT phosphoserine-binding pocket~~, ~~while~~ the ~~interface between the repeats forms a hydrophobic groove that recognizes the phenylalanine~~. ~~Crystallographic and biochemical data suggest that the structural integrity of both binding sites is essential for peptide recognition. The diminished peptide~~-~~binding capacity observed for cancer~~-~~associated BRCA1-BRCT variants may explain the enhanced cancer risks associated with these mutations.~~

The line below this paragraph, {{ABSTRACT_PUBMED_15133503}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15133503 is the PubMed ID number.

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==Disease==

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[[Category: Missense mutation]]

[[Category: Phosphopeptide]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 09~~:26:50 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:21:16 2008''

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-[[Image:1t2v.gif|left|200px]]
+{{Seed}}
+[[Image:1t2v.png|left|200px]]
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 {{STRUCTURE_1t2v|  PDB=1t2v  |  SCENE=  }}
-'''Structural basis of phospho-peptide recognition by the BRCT domain of BRCA1, structure with phosphopeptide'''
+===Structural basis of phospho-peptide recognition by the BRCT domain of BRCA1, structure with phosphopeptide===
-==Overview==
+<!--
-The BRCT repeats in BRCA1 are essential for its tumor suppressor activity and interact with phosphorylated protein targets containing the sequence pSer-X-X-Phe, where X indicates any residue. The structure of the tandem BRCA1 BRCT repeats bound to an optimized phosphopeptide reveals that the N-terminal repeat harbors a conserved BRCT phosphoserine-binding pocket, while the interface between the repeats forms a hydrophobic groove that recognizes the phenylalanine. Crystallographic and biochemical data suggest that the structural integrity of both binding sites is essential for peptide recognition. The diminished peptide-binding capacity observed for cancer-associated BRCA1-BRCT variants may explain the enhanced cancer risks associated with these mutations.
+The line below this paragraph, {{ABSTRACT_PUBMED_15133503}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15133503 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15133503}}
 ==Disease==
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 [[Category: Missense mutation]]
 [[Category: Phosphopeptide]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:26:50 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:21:16 2008''