1fyn

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[[Image:1fyn.gif|left|200px]]
[[Image:1fyn.gif|left|200px]]
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{{Structure
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|PDB= 1fyn |SIZE=350|CAPTION= <scene name='initialview01'>1fyn</scene>, resolution 2.30&Aring;
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The line below this paragraph, containing "STRUCTURE_1fyn", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] </span>
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|GENE= FYN TYROSINE KINASE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_1fyn| PDB=1fyn | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fyn OCA], [http://www.ebi.ac.uk/pdbsum/1fyn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fyn RCSB]</span>
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'''PHOSPHOTRANSFERASE'''
'''PHOSPHOTRANSFERASE'''
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[[Category: Saraste, M.]]
[[Category: Saraste, M.]]
[[Category: Wilmanns, M.]]
[[Category: Wilmanns, M.]]
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[[Category: atp-binding]]
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[[Category: Atp-binding]]
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[[Category: complex (phosphotransferase/peptide)]]
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[[Category: Myristylation]]
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[[Category: myristylation]]
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[[Category: Phosphorylation]]
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[[Category: phosphorylation]]
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[[Category: Proto-oncogene]]
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[[Category: proto-oncogene]]
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[[Category: Sh3 domain]]
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[[Category: sh3 domain]]
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[[Category: Transferase]]
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[[Category: transferase]]
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[[Category: Tyrosine-protein kinase]]
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[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:32:49 2008''
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Revision as of 13:54, 2 May 2008

Template:STRUCTURE 1fyn

PHOSPHOTRANSFERASE


Overview

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.

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 Fri May 2 16:54:47 2008

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