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==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.

==Disease==

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[[Category: oxygen transport]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:18:24 2008''

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@@ Line 4: / Line 4: @@
 ==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.
 ==Disease==
@@ Line 29: / Line 29: @@
 [[Category: oxygen transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:58:48 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:18:24 2008''