Canonical inhibitor-like interactions explain reactivity of alpha1-proteinase inhibitor Pittsburgh and antithrombin with proteinases (Q24308401)

1

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Miljan Simonovic

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Karl Volz

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Peter G W Gettins

Journal of Biological Chemistry

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language of work or name

English

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publication date

26 September 2003

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published in

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volume

278

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issue

39

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page(s)

37881-7

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cites work

Mutation of antitrypsin to antithrombin. alpha 1-antitrypsin Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder

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Mechanism of heparin activation of antithrombin. Evidence for reactive center loop preinsertion with expulsion upon heparin binding

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The anticoagulant activation of antithrombin by heparin

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

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Biological implications of a 3 A structure of dimeric antithrombin

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High-level bacterial expression and 15N-alanine-labeling of bovine trypsin. Application to the study of trypsin-inhibitor complexes and trypsinogen activation by NMR spectroscopy

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The serpin inhibitory mechanism is critically dependent on the length of the reactive center loop

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Inhibitory conformation of the reactive loop of alpha 1-antitrypsin

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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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Natural protein proteinase inhibitors and their interaction with proteinases

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The structure of a Michaelis serpin-protease complex

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Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism

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The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin

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Mapping of the catalytic groove preferences of factor Xa reveals an inadequate selectivity for its macromolecule substrates.

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Serpin structure, mechanism, and function

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Conformational equilibrium of the reactive center loop of antithrombin examined by steady state and time-resolved fluorescence measurements: consequences for the mechanism of factor Xa inhibition by antithrombin-heparin complexes

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Crystal structure of human PEDF, a potent anti-angiogenic and neurite growth-promoting factor

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

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Heparin enhances the specificity of antithrombin for thrombin and factor Xa independent of the reactive center loop sequence. Evidence for an exosite determinant of factor Xa specificity in heparin-activated antithrombin

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Kinetic studies on the interaction of alpha 1-proteinase inhibitor (Pittsburgh) with trypsin-like serine proteinases

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Probing the native strain iin alpha1-antitrypsin

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Formation of a noncovalent serpin-proteinase complex involves no conformational change in the serpin. Use of 1H-15N HSQC NMR as a sensitive nonperturbing monitor of conformation

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release_soy4kdakmvepfeqckyg4q62kdq

21 January 2018

Identifiers

DOI

10.1074/JBC.M305195200

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Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/soy4kdakmvepfeqckyg4q62kdq