The crystal structure of plasminogen activator inhibitor 2 at 2.0 A resolution: implications for serpin function (Q27618604)

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L Jankova

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M Coles

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D Jardine

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J S Whittaker

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A R Gould

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A Meister

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G C King

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B C Mabbutt

Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function

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language of work or name

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15 January 1999

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published in

Structure

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volume

7

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issue

1

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page(s)

43-54

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cites work

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Crystal structure of ovalbumin as a model for the reactive centre of serpins

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Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop

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On the size of the active site in proteases. I. Papain

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Crystal structure of uncleaved ovalbumin at 1.95 A resolution

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Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution

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The ovalbumin family of serpin proteins

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Inhibitory conformation of the reactive loop of alpha 1-antitrypsin

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Protein inhibitors of proteinases

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Natural protein proteinase inhibitors and their interaction with proteinases

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A 1H NMR probe for mobility in the reactive center loops of serpins: spin-echo studies of native and modified forms of ovalbumin and alpha 1-proteinase inhibitor

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Conformation of the reactive site loop of alpha 1-proteinase inhibitor probed by limited proteolysis

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Probing serpin reactive-loop conformations by proteolytic cleavage

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Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins

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Amino acid substitution Glu→Lys in α1-antitrypsin PiZ

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

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

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An analysis of side chain interactions and pair correlations within antiparallel beta-sheets: the differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs.

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Guidelines for protein design: the energetics of beta sheet side chain interactions

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Biological implications of a 3 A structure of dimeric antithrombin

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

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The inhibition mechanism of serpins. Evidence that the mobile reactive center loop is cleaved in the native protease-inhibitor complex.

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

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Role of the catalytic serine in the interactions of serine proteinases with protein inhibitors of the serpin family. Contribution of a covalent interaction to the binding energy of serpin-proteinase complexes.

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Modeling of serpin-protease complexes: antithrombin-thrombin, alpha 1-antitrypsin (358Met-->Arg)-thrombin, alpha 1-antitrypsin (358Met-->Arg)-trypsin, and antitrypsin-elastase

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

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Inhibitory activity and conformational transition of alpha1-proteinase inhibitor variants

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Evidence for the extent of insertion of the active site loop of intact alpha 1 proteinase inhibitor in beta-sheet A

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Immunological Detection of Conformational Neoepitopes Associated with the Serpin Activity of Plasminogen Activator Inhibitor Type-2

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Interfering with the inhibitory mechanism of serpins: crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide

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Structural insights into serpin-protease complexes reveal the inhibitory mechanism of serpins

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Major proteinase movement upon stable serpin-proteinase complex formation

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The structural puzzle of how serpin serine proteinase inhibitors work

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Structural basis for serpin inhibitor activity

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Distortion of the active site of chymotrypsin complexed with a serpin

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Selection of representative protein data sets

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