2PRF
THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I
2PRF の概要
| エントリーDOI | 10.2210/pdb2prf/pdb |
| 分子名称 | PROFILIN IA (1 entity in total) |
| 機能のキーワード | actin-binding |
| 由来する生物種 | Acanthamoeba sp. |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 12962.45 |
| 構造登録者 | Archer, S.J.,Vinson, V.K.,Pollard, T.D.,Lattman, E.E.,Torchia, D.A. (登録日: 1994-01-12, 公開日: 1994-05-31, 最終更新日: 2024-05-01) |
| 主引用文献 | Vinson, V.K.,Archer, S.J.,Lattman, E.E.,Pollard, T.D.,Torchia, D.A. Three-dimensional solution structure of Acanthamoeba profilin-I. J.Cell Biol., 122:1277-1283, 1993 Cited by PubMed Abstract: We have determined a medium resolution three-dimensional solution structure of Acanthamoeba profilin-I by multidimensional nuclear magnetic resonance spectroscopy. This 13-kD actin binding protein consists of a five stranded antiparallel beta sheet flanked by NH2- and COOH-terminal helices on one face and by a third helix and a two stranded beta sheet on the other face. Data from actin-profilin cross-linking experiments and the localization of conserved residues between profilins in different phyla indicate that actin binding occurs on the molecular face occupied by the terminal helices. The other face of the molecule contains the residues that differ between Acanthamoeba profilins-I and II and may be important in determining the difference in polyphosphoinositide binding between these isoforms. This suggests that lipids and actin bind to different faces of the molecule. PubMed: 8397216DOI: 10.1083/jcb.122.6.1277 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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