1BUW

CRYSTAL STRUCTURE OF S-NITROSO-NITROSYL HUMAN HEMOGLOBIN A

1BUW の概要

• エントリーDOI: 10.2210/pdb1buw/pdb
• 分子名称: PROTEIN (HEMOGLOBIN), PROTOPORPHYRIN IX CONTAINING FE, NITRIC OXIDE, ... (5 entities in total)
• 機能のキーワード: oxygen transport and vasodilation, oxygen storage-transport complex, oxygen storage/transport
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 64725.07

構造登録者

Chan, N.-L.,Rogers, P.H.,Arnone, A. (登録日: 1998-09-06, 公開日: 1998-09-16, 最終更新日: 2024-10-30)

主引用文献

Chan, N.L.,Rogers, P.H.,Arnone, A.
Crystal structure of the S-nitroso form of liganded human hemoglobin.
Biochemistry, 37:16459-16464, 1998

PubMed Abstract: Although numerous reports have documented that the S-nitrosylation of cysteine residues by NO alters the activities of a wide variety of proteins, the direct visualization and the structural consequences of this reversible modification have not yet been reported for any protein. Here we describe the crystal structure of S-nitroso-nitrosylhemoglobin determined at a resolution of 1.8 A. The specific reaction of NO with Cys93beta is confirmed in this structure, and a large S-nitrosylation-induced change in the tertiary structure of the COOH-terminal dipeptides of the beta subunits provides additional insight into the stereochemical mechanism by which blood flow is regulated by the interaction of NO with hemoglobin.

PubMed: 9843411
DOI: 10.1021/bi9816711

実験手法

X-RAY DIFFRACTION (1.9 Å)