1fyn: Difference between revisions
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'''PHOSPHOTRANSFERASE''' | '''PHOSPHOTRANSFERASE''' | ||
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[[Category: Saraste, M.]] | [[Category: Saraste, M.]] | ||
[[Category: Wilmanns, M.]] | [[Category: Wilmanns, M.]] | ||
[[Category: | [[Category: Atp-binding]] | ||
[[Category: | [[Category: Myristylation]] | ||
[[Category: | [[Category: Phosphorylation]] | ||
[[Category: | [[Category: Proto-oncogene]] | ||
[[Category: Sh3 domain]] | |||
[[Category: | [[Category: Transferase]] | ||
[[Category: | [[Category: Tyrosine-protein kinase]] | ||
[[Category: | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:54:47 2008'' | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 16:54, 2 May 2008
PHOSPHOTRANSFERASE
OverviewOverview
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 StructureAbout this Structure
1FYN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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