3CYS

DETERMINATION OF THE NMR SOLUTION STRUCTURE OF THE CYCLOPHILIN A-CYCLOSPORIN A COMPLEX

「2CYS」から置き換えられました

3CYS の概要

• エントリーDOI: 10.2210/pdb3cys/pdb
• 関連するPDBエントリー: 1BCK 1C5F 1CSA 1CWA 1CWB 1CWC 1CWF 1CWH 1CWI 1CWJ 1CWK 1CWL 1CWM 1CWO 1CYA 1CYB 1CYN 1IKF 1M63 1MF8 1MIK 1QNG 1QNH 1XQ7 2ESL 2OJU 2POY 2RMA 2RMB 2RMC 2WFJ 2X2C 2X7K 2Z6W 3BO7 3EOV
• 関連するBIRD辞書のPRD_ID: PRD_000142
• 分子名称: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A, CYCLOSPORIN A (2 entities in total)
• 機能のキーワード: isomerase-immunosuppressant complex, cyclophilin-cyclosporin complex, cyclosporin a, immunosuppressant, cyclophilin, isomerase/immunosuppressant
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19257.13

構造登録者

Spitzfaden, C.,Braun, W.,Wider, G.,Widmer, H.,Wuthrich, K. (登録日: 1994-02-28, 公開日: 1994-08-31, 最終更新日: 2025-03-26)

主引用文献

Spitzfaden, C.,Braun, W.,Wider, G.,Widmer, H.,Wuthrich, K.
Determination of the NMR Solution Structure of the Cyclophilin A-Cyclosporin a Complex.
J.Biomol.NMR, 4:463-, 1994

PubMed Abstract: The three-dimensional NMR solution structure of the cyclophilin A (Cyp)-cyclosporin A (CsA) complex was determined, and here we provide a detailed description of the analysis of the NMR data and the structure calculation. Using 15N- and 13C-resolved three- and four-dimensional [1H,1H]-nuclear Overhauser enhancement (NOE) spectroscopy with uniformly isotope-labeled Cyp in the complex, a final data set of 1810 intra-Cyp, 107 intra-CsA and 63 intermolecular NOE upper distance constraints was collected as input for the structure calculation with the program DIANA. A group of DIANA conformers, selected by a previously described analysis of the dependence of the maximal root-mean-square deviation (rmsd) among the individual conformers on the residual target function value, was subjected to energy refinement with the program FANTOM. The 22 best energy-refined conformers were then used to represent the solution structure. The average rmsd relative to the mean structure of these 22 conformers is 1.1 A for the backbone atoms of all residues of the complex. The molecular architecture of Cyp in the Cyp-CsA complex includes an eight-stranded antiparallel beta-barrel, which is closed on each side by an amphipathic helix. CsA is bound in a cavity formed by part of the barrel surface and four loops with nonregular secondary structure. Comparison of this structure with structures of Cyp-CsA and other Cyp-peptide complexes determined by different approaches shows extensive similarities.

PubMed: 8075536
DOI: 10.1007/BF00156614

実験手法

SOLUTION NMR