1FYN

PHOSPHOTRANSFERASE

Summary for 1FYN

• Entry DOI: 10.2210/pdb1fyn/pdb
• Descriptor: PHOSPHOTRANSFERASE FYN, 3BP-2 (3 entities in total)
• Functional Keywords: proto-oncogene, transferase, tyrosine-protein kinase, phosphorylation, atp-binding, myristylation, sh3 domain, complex (phosphotransferase-peptide)
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane: P06241
• Total number of polymer chains: 2
• Total formula weight: 7984.69

Authors

Musacchio, A.,Saraste, M.,Wilmanns, M. (deposition date: 1995-05-17, release date: 1996-11-08, Last modification date: 2024-02-07)

Primary citation

Musacchio, A.,Saraste, M.,Wilmanns, M.
High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides.
Nat.Struct.Biol., 1:546-551, 1994

PubMed Abstract: 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.

PubMed: 7664083
DOI: 10.1038/nsb0894-546

Experimental method

X-RAY DIFFRACTION (2.3 Å)