Title : The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity.

Pub. Date : 2004 Dec 14

PMID : 15548613






4 Functional Relationships(s)
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1 The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity. Heme neuroglobin Mus musculus
2 Unlike in Mb, in Ngb the sixth coordination position of the heme iron is occupied by the distal histidine, in the absence of an exogenous ligand. Heme neuroglobin Mus musculus
3 The heme relocation is accompanied by a significant decrease of structural disorder, especially of the EF loop, which may be the signal whereby Ngb communicates hypoxic conditions. Heme neuroglobin Mus musculus
4 This unexpected structural change unveils a heme-sliding mechanism of affinity control that may be of significance to understanding Ngb"s role in the pathophysiology of the brain. Heme neuroglobin Mus musculus