An atlas of serpin conformations

James Whisstock; Richard Skinner; Arthur Lesk

doi:10.1016/S0968-0004(97)01172-9

An atlas of serpin conformations

James Whisstock, Richard Skinner, Arthur Lesk

Biochemistry & Molecular Biology

Research output: Contribution to journal › Review article › peer-review

163 Scopus citations

Abstract

The serpins are a family of proteins that inhibit chymotrypsin-like serine proteinases, with an unusual mechanism involving a large conformational change known as the stressed→relaxed (S→R) transition. This article is a guide to the known serpin conformations and their biological significance.

Original language	English (US)
Pages (from-to)	63-67
Number of pages	5
Journal	Trends in Biochemical Sciences
Volume	23
Issue number	2
DOIs	https://doi.org/10.1016/S0968-0004(97)01172-9
State	Published - Jan 1 1998

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology

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10.1016/S0968-0004(97)01172-9

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title = "An atlas of serpin conformations",

abstract = "The serpins are a family of proteins that inhibit chymotrypsin-like serine proteinases, with an unusual mechanism involving a large conformational change known as the stressed→relaxed (S→R) transition. This article is a guide to the known serpin conformations and their biological significance.",

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AB - The serpins are a family of proteins that inhibit chymotrypsin-like serine proteinases, with an unusual mechanism involving a large conformational change known as the stressed→relaxed (S→R) transition. This article is a guide to the known serpin conformations and their biological significance.

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An atlas of serpin conformations

Abstract

All Science Journal Classification (ASJC) codes

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