The crystal structure of wild-type human brain neuroglobin reveals flexibility of the disulfide bond that regulates oxygen affinity

Acta Crystallographica Section D: Biological Crystallography

Volumn 70, Issue 4, 2014, Pages 1005-1014

  Guimarães, Beatriz G ^a   Hamdane, Djemel ^b,c   Lechauve, Christophe ^d   Marden, Michael C ^d   Golinelli Pimpaneau, Béatrice ^b,c  

^a SYNCHROTRON SOLEIL   (France)

^b LABORATOIRE D ENZYMOLOGIE ET BIOCHIMIE STRUCTURALES   (France)

^c Paris Sciences et Lettres   (France)

^d INSERM   (France)

Author keywords

disulfide bonds; globins; neuroglobin; oxygen homeostasis; regulatory switch

Indexed keywords

DISULFIDE; GLOBIN; NERVE PROTEIN; NEUROGLOBIN; OXYGEN;

CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; STRUCTURAL HOMOLOGY; X RAY CRYSTALLOGRAPHY;

CRYSTALLOGRAPHY, X-RAY; DISULFIDES; GLOBINS; HUMANS; MODELS, MOLECULAR; NERVE TISSUE PROTEINS; OXYGEN; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; STRUCTURAL HOMOLOGY, PROTEIN;

EID: 84898730883     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S1399004714000078     Document Type: Article

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