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The 1.5 Å Crystal Structure of a Prokaryote Serpin
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title
The 1.5 Å Crystal Structure of a Prokaryote Serpin
(English)
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main subject
crystal structure
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inferred from title
author
Jamie Rossjohn
object named as
Jamie Rossjohn
series ordinal
3
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Stephen P Bottomley
series ordinal
5
object named as
Stephen P. Bottomley
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author name string
James A. Irving
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1
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Lisa D. Cabrita
series ordinal
2
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Robert N. Pike
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4
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James C. Whisstock
series ordinal
6
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language of work or name
English
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publication date
April 2003
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published in
Structure
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volume
11
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issue
4
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page(s)
387-397
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cites work
Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function.
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The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature
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Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen 1: a kinetic analysis
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Ovalbumin and angiotensinogen lack serpin S-R conformational change
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Crystal structure of uncleaved ovalbumin at 1.95 A resolution
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Conformational changes in serpins: I. The native and cleaved conformations of alpha(1)-antitrypsin
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The pH dependence of serpin-proteinase complex dissociation reveals a mechanism of complex stabilization involving inactive and active conformational states of the proteinase which are perturbable by calcium
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Intrinsic fluorescence changes and rapid kinetics of proteinase deformation during serpin inhibition
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Serpin-protease complexes are trapped as stable acyl-enzyme intermediates
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Structure of a serpin-protease complex shows inhibition by deformation
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Heterogeneity in serpin-protease complexes as demonstrated by differences in the mechanism of complex breakdown
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Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins
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Principles that govern the folding of protein chains
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The F-helix of serpins plays an essential, active role in the proteinase inhibition mechanism
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Structural basis of latency in plasminogen activator inhibitor-1
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The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site
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Biological implications of a 3 A structure of dimeric antithrombin
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The intact and cleaved human antithrombin III complex as a model for serpin–proteinase interactions
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The anticoagulant activation of antithrombin by heparin
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Conformational changes in serpins: II. The mechanism of activation of antithrombin by heparin.
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Conformation of the reactive site loop of alpha 1-proteinase inhibitor probed by limited proteolysis
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Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A Linkage
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A 2.6 A structure of a serpin polymer and implications for conformational disease
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Cleaved antitrypsin polymers at atomic resolution
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The mechanism of Z alpha 1-antitrypsin accumulation in the liver
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Effect of the Z mutation on the physical and inhibitory properties of alpha 1-antitrypsin
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Plasminogen-activator inhibitor type 2 (PAI-2) is a spontaneously polymerising SERPIN. Biochemical characterisation of the recombinant intracellular and extracellular forms
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Molecular and structural characterization of the heat-resistant thyroxine-binding globulin-Chicago
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Identification of positively charged residues contributing to the stability of plasminogen activator inhibitor 1
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Serpins in prokaryotes
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Partitioning of serpin-proteinase reactions between stable inhibition and substrate cleavage is regulated by the rate of serpin reactive center loop insertion into beta-sheet A.
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A Kinetic Mechanism for the Polymerization of α1-Antitrypsin
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7 January 2021
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10.1016/S0969-2126(03)00057-1
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