1oj6: Difference between revisions

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[[Image:1oj6.gif|left|200px]]
[[Image:1oj6.gif|left|200px]]


{{Structure
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|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oj6 OCA], [http://www.ebi.ac.uk/pdbsum/1oj6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oj6 RCSB]</span>
}}


'''HUMAN BRAIN NEUROGLOBIN THREE-DIMENSIONAL STRUCTURE'''
'''HUMAN BRAIN NEUROGLOBIN THREE-DIMENSIONAL STRUCTURE'''
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[[Category: Neuroglobin]]
[[Category: Neuroglobin]]
[[Category: Oxygen transport]]
[[Category: Oxygen transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:54:43 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 6 08:02:31 2008''

Revision as of 03:54, 3 May 2008

File:1oj6.gif

Template:STRUCTURE 1oj6

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. 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 Page seeded by OCA on Sat May 3 03:54:43 2008

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