1CF0

HUMAN PLATELET PROFILIN COMPLEXED WITH AN L-PRO10-IODOTYROSINE PEPTIDE

Summary for 1CF0

• Entry DOI: 10.2210/pdb1cf0/pdb
• Descriptor: PROTEIN (PROFILIN), PROTEIN (L-PRO10-IODOTYROSINE) (3 entities in total)
• Functional Keywords: complex (actin-binding protein-peptide), profilin, poly-l-proline, actin cytoskeleton, complex (actin-binding protein-peptide) complex, complex (actin-binding protein/peptide)
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 30821.89

Authors

Rozwarski, D.A.,Mahoney, N.M.,Almo, S.C. (deposition date: 1999-03-23, release date: 1999-07-06, Last modification date: 2023-12-27)

Primary citation

Mahoney, N.M.,Rozwarski, D.A.,Fedorov, E.,Fedorov, A.A.,Almo, S.C.
Profilin binds proline-rich ligands in two distinct amide backbone orientations.
Nat.Struct.Biol., 6:666-671, 1999

PubMed Abstract: The actin regulatory protein profilin is targeted to specific cellular regions through interactions with highly proline-rich motifs embedded within its binding partners. New X-ray crystallographic results demonstrate that profilin, like SH3 domains, can bind proline-rich ligands in two distinct amide backbone orientations. By further analogy with SH3 domains, these data suggest that non-proline residues in profilin ligands may dictate the polarity and register of binding, and the detailed organization of the assemblies involving profilin. This degeneracy may be a general feature of modules that bind proline-rich ligands, including WW and EVH1 domains, and has implications for the assembly and activity of macromolecular complexes involved in signaling and the regulation of the actin cytoskeleton.

PubMed: 10404225
DOI: 10.1038/10722

Experimental method

X-RAY DIFFRACTION (2.2 Å)