1fyn: Difference between revisions
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[[Image:1fyn.gif|left|200px]] | [[Image:1fyn.gif|left|200px]] | ||
'''PHOSPHOTRANSFERASE''' | {{Structure | ||
|PDB= 1fyn |SIZE=350|CAPTION= <scene name='initialview01'>1fyn</scene>, resolution 2.30Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [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] | |||
|GENE= FYN TYROSINE KINASE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''PHOSPHOTRANSFERASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1FYN is a [ | 1FYN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FYN OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7664083 7664083] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tyrosine-protein kinase]] | [[Category: tyrosine-protein kinase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:15:43 2008'' |
Revision as of 12:15, 20 March 2008
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, resolution 2.30Å | |||||||
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Gene: | FYN TYROSINE KINASE (Homo sapiens) | ||||||
Activity: | Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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
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