1oj6
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1oj6.gif|left|200px]] | + | [[Image:1oj6.gif|left|200px]] |
| - | + | ||
| - | '''HUMAN BRAIN NEUROGLOBIN THREE-DIMENSIONAL STRUCTURE''' | + | {{Structure |
| + | |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> | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN BRAIN NEUROGLOBIN THREE-DIMENSIONAL STRUCTURE''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 10: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1OJ6 is a [ | + | 1OJ6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OJ6 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12962627 12962627] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ascenzi, P.]] | [[Category: Ascenzi, P.]] | ||
| Line 29: | Line 38: | ||
[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:11:35 2008'' |
Revision as of 11:11, 20 March 2008
| |||||||
| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. 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
Page seeded by OCA on Thu Mar 20 13:11:35 2008
