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1fyn

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[[Image:1fyn.gif|left|200px]]
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{{STRUCTURE_1fyn| PDB=1fyn | SCENE= }}
{{STRUCTURE_1fyn| PDB=1fyn | SCENE= }}
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'''PHOSPHOTRANSFERASE'''
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===PHOSPHOTRANSFERASE===
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==Overview==
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Src-homology 3 (SH3) domains bind to proline-rich motifs in target proteins. We have determined high-resolution crystal structures of the complexes between the SH3 domains of Abl and Fyn tyrosine kinases, and two ten-residue proline-rich peptides derived from the SH3-binding proteins 3BP-1 and 3BP-2. The X-ray data show that the basic mode of binding of both proline-rich peptides is the same. Peptides are bound over their entire length and interact with three major sites on the SH3 molecules by both hydrogen-bonding and van der Waals contacts. Residues 4-10 of the peptide adopt the conformation of a left-handed polyproline helix type II. Binding of the proline at position 2 requires a kink at the non-proline position 3.
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(as it appears on PubMed at http://www.pubmed.gov), where 7664083 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7664083}}
==About this Structure==
==About this Structure==
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[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Tyrosine-protein kinase]]
[[Category: Tyrosine-protein kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:54:47 2008''
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Revision as of 01:08, 1 July 2008

Template:STRUCTURE 1fyn

PHOSPHOTRANSFERASE

Template:ABSTRACT PUBMED 7664083

About this Structure

1FYN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides., Musacchio A, Saraste M, Wilmanns M, Nat Struct Biol. 1994 Aug;1(8):546-51. PMID:7664083

Page seeded by OCA on Tue Jul 1 04:08:15 2008

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