1JC6

SOLUTION STRUCTURE OF BUNGARUS FACIATUS IX, A KUNITZ-TYPE CHYMOTRYPSIN INHIBITOR

1JC6 の概要

• エントリーDOI: 10.2210/pdb1jc6/pdb
• NMR情報: BMRB: 5050
• 分子名称: VENOM BASIC PROTEASE INHIBITORS IX AND VIIIB (1 entity in total)
• 機能のキーワード: snake venom, kunitz inhibitor, protease inhibitor, neurotoxin, solution structure, bf ix, chymotrypsin inhibitor, toxin
• 由来する生物種: Bungarus fasciatus (banded krait)
• 細胞内の位置: Secreted: P25660
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7305.27

構造登録者

Chen, C.,Hsu, C.H.,Su, N.Y.,Chiou, S.H.,Wu, S.H. (登録日: 2001-06-08, 公開日: 2003-06-17, 最終更新日: 2024-11-13)

主引用文献

Chen, C.,Hsu, C.H.,Su, N.Y.,Lin, Y.C.,Chiou, S.H.,Wu, S.H.
Solution structure of a Kunitz-type chymotrypsin inhibitor isolated from the elapid snake Bungarus fasciatus
J.BIOL.CHEM., 276:45079-45087, 2001

PubMed Abstract: Bungarus fasciatus fraction IX (BF9), a chymotrypsin inhibitor, consists of 65 amino acid residues with three disulfide bridges. It was isolated from the snake venom of B. fasciatus by ion-exchange chromatography and belongs to the bovine pancreatic trypsin inhibitor (BPTI)-like superfamily. It showed a dissociation constant of 5.8 x 10(-8) m with alpha-chymotrypsin as measured by a BIAcore binding assay system. The isothermal titration calorimetry revealed a 1:1 binding stoichiometry between this inhibitor and chymotrypsin and apparently no binding with trypsin. We further used CD and NMR to determine the solution structure of this venom-derived chymotrypsin inhibitor. The three-dimensional NMR solution structures of BF9 were determined on the basis of 582 restraints by simulated annealing and energy minimization calculations. The final set of 10 NMR structures was well defined, with average root mean square deviations of 0.47 A for the backbone atoms in the secondary structure regions and 0.86 A for residues The side chains of Phe(23), Tyr(24), Tyr(25), Phe(35), and Phe(47) exhibited many long-range nuclear Overhauser effects and were the principal components of the hydrophobic core in BF9. To gain insight into the structure-function relationships among proteins in the BPTI-like superfamily, we compared the three-dimensional structure of BF9 with three BPTI-like proteins that possess distinct biological functions. These proteins possessed similar secondary structure elements, but the loop regions and beta-turn were different from one another. Based on residues at the functional site of each protein, we suggest that the flexibility, rigidity, and variations of the amino acid residues in both the loop and beta-turn regions are related to their biological functions.

PubMed: 11562364
DOI: 10.1074/jbc.M106182200

実験手法

SOLUTION NMR