1sha: Difference between revisions

Revision as of 05:39, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1sha.png

Template:STRUCTURE 1sha

CRYSTAL STRUCTURE OF THE PHOSPHOTYROSINE RECOGNITION DOMAIN SH2 OF V-SRC COMPLEXED WITH TYROSINE-PHOSPHORYLATED PEPTIDESCRYSTAL STRUCTURE OF THE PHOSPHOTYROSINE RECOGNITION DOMAIN SH2 OF V-SRC COMPLEXED WITH TYROSINE-PHOSPHORYLATED PEPTIDES

Template:ABSTRACT PUBMED 1379696

About this StructureAbout this Structure

1SHA is a Single protein structure of sequence from Rous sarcoma virus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides., Waksman G, Kominos D, Robertson SC, Pant N, Baltimore D, Birge RB, Cowburn D, Hanafusa H, Mayer BJ, Overduin M, et al., Nature. 1992 Aug 20;358(6388):646-53. PMID:1379696

Page seeded by OCA on Mon Jul 28 05:38:54 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1sha.gif|left|200px]]
+{{Seed}}
+[[Image:1sha.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1sha|  PDB=1sha  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE PHOSPHOTYROSINE RECOGNITION DOMAIN SH2 OF V-SRC COMPLEXED WITH TYROSINE-PHOSPHORYLATED PEPTIDES'''
+===CRYSTAL STRUCTURE OF THE PHOSPHOTYROSINE RECOGNITION DOMAIN SH2 OF V-SRC COMPLEXED WITH TYROSINE-PHOSPHORYLATED PEPTIDES===
-==Overview==
+<!--
-Three-dimensional structures of complexes of the SH2 domain of the v-src oncogene product with two phosphotyrosyl peptides have been determined by X-ray crystallography at resolutions of 1.5 and 2.0 A, respectively. A central antiparallel beta-sheet in the structure is flanked by two alpha-helices, with peptide binding mediated by the sheet, intervening loops and one of the helices. The specific recognition of phosphotyrosine involves amino-aromatic interactions between lysine and arginine side chains and the ring system in addition to hydrogen-bonding interactions with the phosphate.
+The line below this paragraph, {{ABSTRACT_PUBMED_1379696}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 1379696 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_1379696}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Waksman, G.]]
 [[Category: Phosphotransferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:42:16 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:38:54 2008''