1oj6
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1OJ6 is a [[Single protein]] structure | + | 1OJ6 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OJ6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Nardini, M.]] | [[Category: Nardini, M.]] | ||
[[Category: Pesce, A.]] | [[Category: Pesce, A.]] | ||
| - | [[Category: | + | [[Category: Heme hexacoordination]] |
| - | [[Category: | + | [[Category: Neuroglobin]] |
| - | [[Category: | + | [[Category: Oxygen transport]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 6 08:02:31 2008'' |
Revision as of 05:02, 6 April 2008
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| , resolution 1.95Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN BRAIN NEUROGLOBIN THREE-DIMENSIONAL STRUCTURE
Overview
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 Structure
1OJ6 is a Single protein structure. Full crystallographic information is available from OCA.
Reference
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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