1fyn: Difference between revisions

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[[Image:1fyn.gif|left|200px]]
{{Seed}}
[[Image:1fyn.png|left|200px]]


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{{STRUCTURE_1fyn|  PDB=1fyn  |  SCENE=  }}  
{{STRUCTURE_1fyn|  PDB=1fyn  |  SCENE=  }}  


'''PHOSPHOTRANSFERASE'''
===PHOSPHOTRANSFERASE===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_7664083}}, adds the Publication Abstract to the page
(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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