The role of strand 1 of the C beta-sheet in the structure and function of alpha(1)-antitrypsin (Q28364511)

ORCID Public Data File 2021

author name string

I D Lawrenson

2

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D Tew

3

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W Dai

4

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J C Whisstock

5

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R N Pike

Structure of a serpin-protease complex shows inhibition by deformation

6

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language of work or name

English

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publication date

December 2001

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published in

Protein Science

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volume

10

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issue

12

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page(s)

2518-24

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cites work

1 reference

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A 2.6 A structure of a serpin polymer and implications for conformational disease

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The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site

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Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpins

20 March 2017

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Inhibitory conformation of the reactive loop of alpha 1-antitrypsin

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The serpin superfamily of proteinase inhibitors: structure, function, and regulation

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Engineering of plasminogen activator inhibitor-1 to reduce the rate of latency transition

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The intact and cleaved human antithrombin III complex as a model for serpin–proteinase interactions

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Pleiotropic effects of antithrombin strand 1C substitution mutations

20 March 2017

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A serpin-induced extensive proteolytic susceptibility of urokinase-type plasminogen activator implicates distortion of the proteinase substrate-binding pocket and oxyanion hole in the serpin inhibitory mechanism

20 March 2017

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Antithrombins Wibble and Wobble (T85M/K): archetypal conformational diseases with in vivo latent-transition, thrombosis, and heparin activation.

29 September 2017

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Wild-type alpha 1-antitrypsin is in the canonical inhibitory conformation.

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Major proteinase movement upon stable serpin-proteinase complex formation

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Structural change in alpha-chymotrypsin induced by complexation with alpha 1-antichymotrypsin as seen by enhanced sensitivity to proteolysis.

29 September 2017

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A fluorescent probe study of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism

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Crucial residues in the carboxy-terminal end of C1 inhibitor revealed by pathogenic mutants impaired in secretion or function

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What do dysfunctional serpins tell us about molecular mobility and disease?

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Congenital antititrombin III deficiency (AT-III Kyoto) : Identification of a point mutation altering arginine-406 to methionine behind the reactive site

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Effects of serpin binding on the target proteinase: global stabilization, localized increased structural flexibility, and conserved hydrogen bonding at the active site.

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COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization

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2 June 2018

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Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site

2 June 2018

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An ester bond linking a fragment of a serine proteinase to its serpin inhibitor.

20 June 2018

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https://api.crossref.org/works/10.1110%2FPS.PS.24101

Alpha 1-proteinase inhibitor variant T345R. Influence of P14 residue on substrate and inhibitory pathways

21 January 2018

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Intrinsic fluorescence changes and rapid kinetics of proteinase deformation during serpin inhibition

21 January 2018

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Comparison of the esterase activities of trypsin, plasmin, and thrombin on guanidinobenzoate esters. Titration of the enzymes

21 January 2018

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12 December 2020

Inhibitory mechanism of serpins. Interaction of thrombin with antithrombin and protease nexin 1

1 reference

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Serpin-protease complexes are trapped as stable acyl-enzyme intermediates

1 reference

12 December 2020

The contribution of the conserved hinge region residues of alpha1-antitrypsin to its reaction with elastase

1 reference

12 December 2020

Inhibitory mechanism of serpins. Identification of steps involving the active-site serine residue of the protease

1 reference

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Inhibitory mechanism of serpins. Mobility of the C-terminal region of the reactive-site loop

1 reference

12 December 2020

Structure-function relationships in serpins: current concepts and controversies

1 reference

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Protein engineering of chimeric Serpins: an investigation into effects of the serpin scaffold and reactive centre loop length

1 reference

12 December 2020