5XG9
Crystal Structure of PEG-bound SH3 domain of Myosin IB from Entamoeba histolytica
5XG9 の概要
エントリーDOI | 10.2210/pdb5xg9/pdb |
関連するPDBエントリー | 5XGG |
分子名称 | Unconventional myosin IB, PENTAETHYLENE GLYCOL, 2,5,8,11,14,17,20,23,26,29,32,35,38,41,44,47,50,53,56,59,62,65,68,71,74,77,80-HEPTACOSAOXADOOCTACONTAN-82-OL, ... (6 entities in total) |
機能のキーワード | sh3, myosini, entamoeba histolytica, peg-bound sh3 complex, contractile protein |
由来する生物種 | Entamoeba histolytica |
タンパク質・核酸の鎖数 | 8 |
化学式量合計 | 65987.82 |
構造登録者 | |
主引用文献 | Gautam, G.,Rehman, S.A.A.,Pandey, P.,Gourinath, S. Crystal structure of the PEG-bound SH3 domain of myosin IB from Entamoeba histolytica reveals its mode of ligand recognition Acta Crystallogr D Struct Biol, 73:672-682, 2017 Cited by PubMed Abstract: The versatility in the recognition of various interacting proteins by the SH3 domain drives a variety of cellular functions. Here, the crystal structure of the C-terminal SH3 domain of myosin IB from Entamoeba histolytica (EhMySH3) is reported at a resolution of 1.7 Å in native and PEG-bound states. Comparisons with other structures indicated that the PEG molecules occupy protein-protein interaction pockets similar to those occupied by the peptides in other peptide-bound SH3-domain structures. Also, analysis of the PEG-bound EhMySH3 structure led to the recognition of two additional pockets, apart from the conventional polyproline and specificity pockets, that are important for ligand interaction. Molecular-docking studies combined with various comparisons revealed structural similarity between EhMySH3 and the SH3 domain of β-Pix, and this similarity led to the prediction that EhMySH3 preferentially binds targets containing type II-like PXXP motifs. These studies expand the understanding of the EhMySH3 domain and provide extensive structural knowledge, which is expected to help in predicting the interacting partners which function together with myosin IB during phagocytosis in E. histolytica infections. PubMed: 28777082DOI: 10.1107/S2059798317009639 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.78 Å) |
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