2ACG
ACANTHAMOEBA CASTELLANII PROFILIN II
2ACG の概要
| エントリーDOI | 10.2210/pdb2acg/pdb |
| 分子名称 | PROFILIN II (2 entities in total) |
| 機能のキーワード | protein binding, profilin, actin-binding protein, contractile protein |
| 由来する生物種 | Acanthamoeba castellanii |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 12937.44 |
| 構造登録者 | Fedorov, A.A.,Magnus, K.A.,Graupe, M.H.,Lattman, E.E.,Pollard, T.D.,Almo, S.C. (登録日: 1994-08-30, 公開日: 1994-11-01, 最終更新日: 2024-02-14) |
| 主引用文献 | Fedorov, A.A.,Magnus, K.A.,Graupe, M.H.,Lattman, E.E.,Pollard, T.D.,Almo, S.C. X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates. Proc.Natl.Acad.Sci.USA, 91:8636-8640, 1994 Cited by PubMed Abstract: We determined the structures of Acanthamoeba profilin I and profilin II by x-ray crystallography at resolutions of 2.0 and 2.8 A, respectively. The polypeptide folds and the actin-binding surfaces of the amoeba profilins are very similar to those of bovine and human profilins. The electrostatic potential surfaces of the two Acanthamoeba isoforms differ. Two areas of high positive potential on the surface of profilin II are candidate binding sites for phosphatidylinositol phosphates. The proximity of these sites to the actin binding site provides an explanation for the competition between actin and lipids for binding profilin. PubMed: 8078936DOI: 10.1073/pnas.91.18.8636 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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