1oj6

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[[Image:1oj6.gif|left|200px]]
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{{Seed}}
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[[Image:1oj6.png|left|200px]]
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{{STRUCTURE_1oj6| PDB=1oj6 | SCENE= }}
{{STRUCTURE_1oj6| PDB=1oj6 | SCENE= }}
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'''HUMAN BRAIN NEUROGLOBIN THREE-DIMENSIONAL STRUCTURE'''
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===HUMAN BRAIN NEUROGLOBIN THREE-DIMENSIONAL STRUCTURE===
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==Overview==
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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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The line below this paragraph, {{ABSTRACT_PUBMED_12962627}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 12962627 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12962627}}
==About this Structure==
==About this Structure==
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[[Category: Neuroglobin]]
[[Category: Neuroglobin]]
[[Category: Oxygen transport]]
[[Category: Oxygen transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:54:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:14:10 2008''

Revision as of 15:14, 27 July 2008

Image:1oj6.png

Template:STRUCTURE 1oj6

HUMAN BRAIN NEUROGLOBIN THREE-DIMENSIONAL STRUCTURE

Template:ABSTRACT PUBMED 12962627

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

Page seeded by OCA on Sun Jul 27 18:14:10 2008

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