1PBA

THE NMR STRUCTURE OF THE ACTIVATION DOMAIN ISOLATED FROM PORCINE PROCARBOXYPEPTIDASE B

1PBA の概要

• エントリーDOI: 10.2210/pdb1pba/pdb
• 分子名称: PROCARBOXYPEPTIDASE B (1 entity in total)
• 機能のキーワード: hydrolase(c-terminal peptidase)
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Secreted: P09955
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9518.36

構造登録者

Vendrell, J.,Wider, G.,Billeter, M.,Aviles, F.X.,Wuthrich, K. (登録日: 1991-11-18, 公開日: 1993-10-31, 最終更新日: 2024-05-22)

主引用文献

Vendrell, J.,Billeter, M.,Wider, G.,Aviles, F.X.,Wuthrich, K.
The NMR structure of the activation domain isolated from porcine procarboxypeptidase B.
EMBO J., 10:11-15, 1991

PubMed Abstract: The three-dimensional structure of the activation domain isolated from porcine pancreatic procarboxypeptidase B was determined using 1H NMR spectroscopy. A group of 20 conformers is used to describe the solution structure of this 81 residue polypeptide chain, which has a well-defined backbone fold from residues 11-76 with an average root mean square distance for the backbone atoms of 1.0 +/- 0.1 A relative to the mean of the 20 conformers. The molecular architecture contains a four-stranded beta-sheet with the polypeptide segments 11-17, 36-39, 50-56 and 75-76, two well defined alpha-helices from residues 20-30 and 60-70, and a 3(10) helix from residues 43-46. The three helices are oriented almost exactly antiparallel to each other, are all on the same side of the beta-sheet, and the helix axes from an angle of approximately 45 degrees relative to the direction of the beta-strands. Three segments linking beta-strands and helical secondary structures, with residues 32-35, 39-43 and 56-61, are significantly less well ordered than the rest of the molecule. In the three-dimensional structure two of these loops (residues 32-35 and 56-61) are located close to each other near the protein surface, forming a continuous region of increased mobility, and the third disordered loop is separated from this region only by the peripheral beta-strand 36-39 and precedes the short 3(10) helix.

PubMed: 1989879

実験手法

SOLUTION NMR