1ABO

CRYSTAL STRUCTURE OF THE COMPLEX OF THE ABL TYROSINE KINASE SH3 DOMAIN WITH 3BP-1 SYNTHETIC PEPTIDE

Summary for 1ABO

• Entry DOI: 10.2210/pdb1abo/pdb
• Descriptor: ABL TYROSINE KINASE, 3BP-1 SYNTHETIC PEPTIDE, 10 RESIDUES, SULFATE ION, ... (4 entities in total)
• Functional Keywords: sh3 domain, transferase (phosphotransferase), proto-oncogene, complex (kinase-peptide) complex, complex (kinase/peptide)
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm, cytoskeleton: P00520
• Total number of polymer chains: 4
• Total formula weight: 15987.76

Authors

Musacchio, A.,Wilmanns, M.,Saraste, M. (deposition date: 1995-05-19, release date: 1995-10-15, 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 Å)