1oj6: Difference between revisions
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|PDB= 1oj6 |SIZE=350|CAPTION= <scene name='initialview01'>1oj6</scene>, resolution 1.95Å | |PDB= 1oj6 |SIZE=350|CAPTION= <scene name='initialview01'>1oj6</scene>, resolution 1.95Å | ||
|SITE= <scene name='pdbsite=AC1:Hem+Binding+Site+For+Chain+D'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Hem+Binding+Site+For+Chain+D'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|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> | |||
}} | }} | ||
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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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Nardini, M.]] | [[Category: Nardini, M.]] | ||
[[Category: Pesce, A.]] | [[Category: Pesce, A.]] | ||
[[Category: heme hexacoordination]] | [[Category: heme hexacoordination]] | ||
[[Category: neuroglobin]] | [[Category: neuroglobin]] | ||
[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:46:07 2008'' | ||
Revision as of 22:46, 30 March 2008
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| , resolution 1.95Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. 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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