Literature DB >> 20211924

Replacement of Phe274 with conserved residue Tyr274 for reactive center loop expulsion in antithrombin.

Urmila Duhan1.   

Abstract

BACKGROUND: The reactive center loop (RCL) of native antithrombin is partially inserted in the main serpin body. It must be fully exposed for optimal inhibitory function.
OBJECTIVE: To test the hypothesis that P(14)-s2B interaction affects loop insertion in antithrombin. By mutating Phe(274) to Tyr(274), the objective was to introduce P(14)-s2B interaction in antithrombin.
METHODS: Site-directed mutagenesis and affinity chromatography were used to obtain purified recombinant protein. Antithrombin's ability to form sodium dodecyl sulfate (SDS)-stable complex with thrombin, stoichiometry of thrombin inhibition, second-order rate constant for thrombin and factor Xa (fXa) inhibition (M(-1) s(-1)), and heparin dissociation constant (K(D); tryptophan fluorescence emission spectra) were determined. RESULTS AND
CONCLUSION: A marginal, but inconclusive, difference between the wild type and the mutant was observed. The result highlights the variable effect of P(14)-s2B interaction in different serpins. Alternate hypothesis for achieving loop expulsion is proposed.

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Year:  2010        PMID: 20211924      PMCID: PMC3828558          DOI: 10.1177/1076029609360529

Source DB:  PubMed          Journal:  Clin Appl Thromb Hemost        ISSN: 1076-0296            Impact factor:   2.389


  14 in total

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Authors:  A Futamura; P G Gettins
Journal:  J Biol Chem       Date:  2000-02-11       Impact factor: 5.157

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Authors:  V Arocas; B Turk; S C Bock; S T Olson; I Björk
Journal:  Biochemistry       Date:  2000-07-25       Impact factor: 3.162

7.  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.

Authors:  Gonzalo Izaguirre; Steven T Olson
Journal:  J Biol Chem       Date:  2006-03-03       Impact factor: 5.157

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