1oj6: Difference between revisions
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Revision as of 17:51, 5 November 2007
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HUMAN BRAIN NEUROGLOBIN THREE-DIMENSIONAL STRUCTURE
OverviewOverview
Neuroglobin, mainly expressed in vertebrate brain and retina, is a, recently identified member of the globin superfamily. Augmenting O(2), supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. In the absence of exogenous ligands, neuroglobin displays a hexacoordinated heme. O(2) and CO bind to the heme, iron, displacing the endogenous HisE7 heme distal ligand. Hexacoordinated, human neuroglobin displays a classical globin fold adapted to host the, reversible bis-histidyl heme complex and an elongated protein matrix, cavity, held to facilitate O(2) diffusion to the heme. The neuroglobin, structure suggests that the classical globin fold is endowed with striking, adaptability, indicating that hemoglobin and myoglobin are just two, examples within a wide and functionally diversified protein homology, superfamily.
About this StructureAbout this Structure
1OJ6 is a Single protein structure of sequence from [1] with SO4 and HEM as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity., Pesce A, Dewilde S, Nardini M, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M, Structure. 2003 Sep;11(9):1087-95. PMID:12962627
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