1CJF
PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS
Summary for 1CJF
| Entry DOI | 10.2210/pdb1cjf/pdb |
| Descriptor | PROTEIN (HUMAN PLATELET PROFILIN), PROTEIN (PROLINE PEPTIDE), 7-HYDROXY-4-METHYL-3-(2-HYDROXY-ETHYL)COUMARIN, ... (4 entities in total) |
| Functional Keywords | profilin, actin-binding protein, cytoskeleton, poly-l-proline, structural regulation protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 33269.96 |
| Authors | Mahoney, N.M.,Fedorov, A.A.,Fedorov, E.,Rozwarski, D.A.,Almo, S.C. (deposition date: 1999-04-13, release date: 1999-07-07, Last modification date: 2023-08-09) |
| 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 Cited by 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: 10404225DOI: 10.1038/10722 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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