1OA6

The solution structure of bovine pancreatic trypsin inhibitor at high pressure

1OA6 の概要

• エントリーDOI: 10.2210/pdb1oa6/pdb
• 関連するPDBエントリー: 1AAL 1B0C 1BHC 1BPI 1BPT 1BTH 1BTI 1BZ5 1BZX 1CBW 1D0D 1EAW 1EJM 1F5R 1F7Z 1FAN 1FY8 1G6X 1JV8 1JV9 1K6U 1LD5 1LD6 1MTN 1NAG 1OA5 1PIT 1QLQ 1TPA 2HEX 2KAI 2PTC 2TGP 2TPI 3BTD 3BTE 3BTF 3BTG 3BTH 3BTK 3BTM 3BTQ 3BTT 3BTW 3TGI 3TGJ 3TGK 3TPI 4PTI 4TPI 5PTI 6PTI 7PTI 8PTI 9PTI
• 分子名称: PANCREATIC TRYPSIN INHIBITOR (2 entities in total)
• 機能のキーワード: hydrolase inhibitor, protease inhibitor
• 由来する生物種: BOS TAURUS (BOVINE)
• 細胞内の位置: Secreted: P00974
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6527.57

構造登録者

Williamson, M.P.,Akasaka, K.,Refaee, M. (登録日: 2003-01-02, 公開日: 2003-08-28, 最終更新日: 2024-11-13)

主引用文献

Williamson, M.P.,Akasaka, K.,Refaee, M.
The Solution Structure of Bovine Pancreatic Trypsin Inhibitor at High Pressure
Protein Sci., 12:1971-, 2003

PubMed Abstract: The solution structure of bovine pancreatic trypsin inhibitor (BPTI) at a pressure of 2 kbar is presented. The structure was calculated as a change from an energy-minimized low-pressure structure, using (1)H chemical shifts as restraints. The structure has changed by 0.24 A RMS, and has almost unchanged volume. The largest changes as a result of pressure are in the loop 10-16, which contains the active site of BPTI, and residues 38-42, which are adjacent to buried water molecules. Hydrogen bonds are compressed by 0.029 +/- 0.117 A, with the longer hydrogen bonds, including those to internal buried water molecules, being compressed more. The hydrophobic core is also compressed, largely from reduction of packing defects. The parts of the structure that have the greatest change are close to buried water molecules, thus highlighting the importance of water molecules as the nucleation sites for volume fluctuation of proteins in native conditions.

PubMed: 12930996
DOI: 10.1110/PS.0242103

実験手法

SOLUTION NMR