The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity

Proceedings of the National Academy of Sciences of the United States of America

Volumn 101, Issue 50, 2004, Pages 17351-17356

  Vallone, Beatrice ^a   Nienhaus, Karin ^b   Matthes, Annemarie ^b   Brunori, Maurizio ^a   Nienhaus, G Ulrich ^b,c  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

^b UNIVERSITY OF ULM   (Germany)

^c UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

Binding; Conformational changes; Hypoxia signaling; Protein crystallography

Indexed keywords

CARBON MONOXIDE; GLOBULAR PROTEIN; HEME; HISTIDINE; LIGAND; NEUROGLOBIN PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; CRYSTALLIZATION; HYPOXIA; INFRARED SPECTROSCOPY; LIGAND BINDING; MOUSE; NONHUMAN; OXYGEN AFFINITY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; ANIMALS; CARBON MONOXIDE; CRYSTALLOGRAPHY, X-RAY; GLOBINS; HEME; LIGANDS; MICE; MODELS, MOLECULAR; NERVE TISSUE PROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

MURINAE; VERTEBRATA;

EID: 10644251786     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0407633101     Document Type: Article

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