1oj6
From Proteopedia
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==Overview== | ==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. | 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. | ||
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| + | ==Disease== | ||
| + | Known disease associated with this structure: Galactosialidosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=256540 256540]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:33:14 2007'' |
Revision as of 16:26, 12 November 2007
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HUMAN BRAIN NEUROGLOBIN THREE-DIMENSIONAL STRUCTURE
Contents |
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.
Disease
Known disease associated with this structure: Galactosialidosis OMIM:[256540]
About 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.
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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