Solution structure of a protein inhibitor of neuronal nitric oxide synthase

被引：44

作者：

Tochio, H ^{[1
]}

Ohki, S ^{[1
]}

Zhang, Q ^{[1
]}

Li, M ^{[1
]}

Zhang, MJ ^{[1
]}

机构：

[1] Hong Kong Univ Sci & Technol, Dept Biochem, Hong Kong, Peoples R China

来源：

NATURE STRUCTURAL BIOLOGY | 1998年 / 5卷 / 11期

关键词：

D O I：

10.1038/2940

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The structure of the neuronal nitric oxide synthase inhibitory protein, PIN (protein inhibitor of nNOS), has been determined by NMR spectroscopy. Two N-terminal antiparallel alpha-helices pack against a four-stranded antiparallel beta-sheet in the C-terminal region of the protein, forming a two-layer alpha/beta plait. The three dimensional structure of PIN resembles the fold of the B-chain of spartylglucosaminidase. A non-prolyl cis peptide bond was found between Pro 52 and Thr 53 of the protein. PIN has a large solvent-exposed hydrophobic surface that contains a cavity and is rimmed with positive charges. This surface may serve as the primary target-binding region for this multi-functional regulatory protein.

引用

页码：965 / 969

页数：5

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