The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site 1 1Edited by R. Huber

Author:

Skinner Richard,Abrahams Jan-Pieter,Whisstock James C,Lesk Arthur M,Carrell Robin W,Wardell Mark R

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference43 articles.

1. Production in vitro and properties of a modified form of bovine antithrombin, cleaved at the active site by thrombin;Björk;J. Biol. Chem.,1982

2. Arginine 47 is a prime heparin binding site in antithrombin. A new variant Rouen II, 47 Arg to Ser;Borg;J. Clin. Invest.,1988

3. New carbohydrate site in mutant antithrombin (7 Ile-Asn) with decreased heparin affinity;Brennan;FEBS Letters,1988

4. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures;Brünger;Nature,1992

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