The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site

Journal of Molecular Biology

Volumn 266, Issue 3, 1997, Pages 601-609

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

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

Author keywords

2.6 structure; Antithrombin; Dimer; Heparin pentasaccharide binding; X ray crystallography

Indexed keywords

ANTITHROMBIN; DIMER; HEPARIN; HEPARIN BINDING PROTEIN; ANTITHROMBIN III;

ARTICLE; BINDING AFFINITY; BINDING SITE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; HYDROGEN BOND; MICROGRAVITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION; CHEMISTRY; FLIGHT EXPERIMENT; HUMAN; MANNED; METABOLISM; MOLECULAR GENETICS; SHORT DURATION; STS-67 SHUTTLE PROJECT; X RAY CRYSTALLOGRAPHY;

FLIGHT EXPERIMENT; MANNED; SHORT DURATION; STS-67 SHUTTLE PROJECT;

ANTITHROMBIN III; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; HEPARIN; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION;

EID: 0031588685     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0798     Document Type: Article

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