1E6F
Human MIR-receptor, repeat 11
1E6F の概要
エントリーDOI | 10.2210/pdb1e6f/pdb |
分子名称 | CATION-INDEPENDENT MANNOSE-6-PHOSPHATE RECEPTOR (2 entities in total) |
機能のキーワード | receptor, mir-receptor, igf-ii receptor, transport, glycoprotein |
由来する生物種 | HOMO SAPIENS (HUMAN) |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 31129.34 |
構造登録者 | Von Buelow, R.,Rajashankar, K.R.,Dauter, M.,Dauter, Z.,Grimme, S.,Schmidt, B.,Von Figura, K.,Uson, I. (登録日: 2000-08-15, 公開日: 2001-08-09, 最終更新日: 2024-11-13) |
主引用文献 | Uson, I.,Schmidt, B.,Von Buelow, R.,Grimme, S.,Von Figura, K.,Dauter, M.,Rajashankar, K.R.,Dauter, Z.,Sheldrick, G.M. Locating the Anomalous Scatterer Substructures in Halide and Sulfur Phasing Acta Crystallogr.,Sect.D, 59:57-, 2003 Cited by PubMed Abstract: Improved data quality now makes it feasible to exploit the weak anomalous signal derived only from the sulfurs inherent to the protein or in particular from halide ions incorporated by soaking. The latter technique requires the location of a high number of partially occupied halide sites. This number appears to be roughly proportional to the exposed protein surface. This paper explores the application of dual-space ab initio methods as implemented in the program SHELXD to the location of substructures of sulfur in SAD experiments, bromide in SAD and MAD experiments and iodide using SAD and SIRAS to determine the anomalous-atom substructure. Sets of atoms consistent with the Patterson function were generated as a starting point for the dual-space recycling procedure in SHELXD. The substructure is then expanded to the full structure by maximum-likelihood phasing with SHARP and density modification with the program DM. Success in the location of the substructures and subsequent phasing depends critically on the quality of the data and on the extent of the anomalous signal. This varies with each crystal and soak, but for the same crystal the significance of the anomalous signal was found to be highly sensitive to the redundancy of the intensity measurements, which in some cases made all the difference. This is illustrated by the determination of the previously unknown structure of repeat 11 of the human mannose-6-phosphate/insulin-like growth factor II receptor (Man6P/IGFII-receptor), with 310 amino acids in the asymmetric unit, which was phased by soaking the crystals in a cryoprotectant solution containing halide anions. PubMed: 12499540DOI: 10.1107/S090744490201884X 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.75 Å) |
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