3RP2

THE STRUCTURE OF RAT MAST CELL PROTEASE II AT 1.9-ANGSTROMS RESOLUTION

3RP2 の概要

• エントリーDOI: 10.2210/pdb3rp2/pdb
• 分子名称: RAT MAST CELL PROTEASE II (2 entities in total)
• 機能のキーワード: serine proteinase
• 由来する生物種: Rattus rattus (black rat)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49605.63

構造登録者

Reynolds, R.,Remington, S.,Weaver, L.,Fischer, R.,Anderson, W.,Ammon, H.,Matthews, B. (登録日: 1984-09-10, 公開日: 1984-10-29, 最終更新日: 2024-10-23)

主引用文献

Remington, S.J.,Woodbury, R.G.,Reynolds, R.A.,Matthews, B.W.,Neurath, H.
The structure of rat mast cell protease II at 1.9-A resolution.
Biochemistry, 27:8097-8105, 1988

PubMed Abstract: The structure of rat mast cell protease II (RMCP II), a serine protease with chymotrypsin-like primary specificity, has been determined to a nominal resolution of 1.9 A by single isomorphous replacement, molecular replacement, and restrained crystallographic refinement to a final R-factor of 0.191. There are two independent molecules of RMCP II in the asymmetric unit of the crystal. The rms deviation from ideal bond lengths is 0.016 A and from ideal bond angles is 2.7 degrees. The overall structure of RMCP II is extremely similar to that of chymotrypsin, but the largest differences between the two structures are clustered around the active-site region in a manner which suggests that the unusual substrate specificity of RMCP II is due to these changes. Unlike chymotrypsin, RMCP II has a deep cleft around the active site. An insertion of three residues between residues 35 and 41 of chymotrypsin, combined with concerted changes in sequence and a deletion near residue 61, allows residues 35-41 of RMCP II to adopt a conformation not seen in any other serine protease. Additionally, the loss of the disulfide bridge between residues 191 and 220 of chymotrypsin leads to the formation of an additional substrate binding pocket that we propose to interact with the P3 side chain of bound substrate. RMCP II is a member of a homologous subclass of serine proteases that are expressed by mast cells, neutrophils, lymphocytes, and cytotoxic T-cells. Thus, the structure of RMCP II forms a basis for an explanation of the unusual properties of other members of this class.

PubMed: 3233198
DOI: 10.1021/bi00421a019

実験手法

X-RAY DIFFRACTION (1.9 Å)