Residues Tyr253 and Glu255 in strand 3 of beta-sheet C of antithrombin are key determinants of an exosite made accessible by heparin activation to promote rapid inhibition of factors Xa and IXa.
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Molecular basis of factor IXa recognition by heparin-activated antithrombin revealed by a 1.7-A structure of the ternary complexStructural and Functional Characterization of a Highly Specific Serpin in the Insect Innate ImmunityTargeted mutagenesis of zebrafish antithrombin III triggers disseminated intravascular coagulation and thrombosis, revealing insight into function.Role of the residues of the 39-loop in determining the substrate and inhibitor specificity of factor IXa.Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease.Structural and inhibitory effects of hinge loop mutagenesis in serpin-2 from the malaria vector Anopheles gambiae.Role of the C-sheet in the maturation of N-glycans on antithrombin: functional relevance of pleiotropic mutations.Saturation Mutagenesis of the Antithrombin Reactive Center Loop P14 Residue Supports a Three-step Mechanism of Heparin Allosteric Activation Involving Intermediate and Fully Activated StatesThe allosteric mechanism of activation of antithrombin as an inhibitor of factor IXa and factor Xa: heparin-independent full activation through mutations adjacent to helix D.Exosite determinants of serpin specificity.Role of P2 glycine in determining the specificity of antithrombin reaction with coagulation proteases.The signature 3-O-sulfo group of the anticoagulant heparin sequence is critical for heparin binding to antithrombin but is not required for allosteric activation.Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. A paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors.Kinetic evidence that allosteric activation of antithrombin by heparin is mediated by two sequential conformational changes.Characterization of the conformational alterations, reduced anticoagulant activity, and enhanced antiangiogenic activity of prelatent antithrombinInhibitory serpins. New insights into their folding, polymerization, regulation and clearance.Serpins in arthropod biology.Replacement of Phe274 with conserved residue Tyr274 for reactive center loop expulsion in antithrombin.Engineering functional antithrombin exosites in alpha1-proteinase inhibitor that specifically promote the inhibition of factor Xa and factor IXa.Activation of antithrombin as a factor IXa and Xa inhibitor involves mitigation of repression rather than positive enhancement.Disease-causing mutations in the serpin antithrombin reveal a key domain critical for inhibiting protease activities.Dynamic properties of the native free antithrombin from molecular dynamics simulations: computational evidence for solvent- exposed Arg393 side chain.
P2860
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P2860
Residues Tyr253 and Glu255 in strand 3 of beta-sheet C of antithrombin are key determinants of an exosite made accessible by heparin activation to promote rapid inhibition of factors Xa and IXa.
description
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name
Residues Tyr253 and Glu255 in ...... ibition of factors Xa and IXa.
@en
Residues Tyr253 and Glu255 in ...... ibition of factors Xa and IXa.
@nl
type
label
Residues Tyr253 and Glu255 in ...... ibition of factors Xa and IXa.
@en
Residues Tyr253 and Glu255 in ...... ibition of factors Xa and IXa.
@nl
prefLabel
Residues Tyr253 and Glu255 in ...... ibition of factors Xa and IXa.
@en
Residues Tyr253 and Glu255 in ...... ibition of factors Xa and IXa.
@nl
P2860
P356
P1476
Residues Tyr253 and Glu255 in ...... ibition of factors Xa and IXa.
@en
P2093
Gonzalo Izaguirre
Steven T Olson
P2860
P304
13424-13432
P356
10.1074/JBC.M600415200
P407
P577
2006-03-03T00:00:00Z