1CF0
HUMAN PLATELET PROFILIN COMPLEXED WITH AN L-PRO10-IODOTYROSINE PEPTIDE
1CF0 の概要
| エントリーDOI | 10.2210/pdb1cf0/pdb |
| 分子名称 | PROTEIN (PROFILIN), PROTEIN (L-PRO10-IODOTYROSINE) (3 entities in total) |
| 機能のキーワード | complex (actin-binding protein-peptide), profilin, poly-l-proline, actin cytoskeleton, complex (actin-binding protein-peptide) complex, complex (actin-binding protein/peptide) |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 30821.89 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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