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1cmy
From Proteopedia
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THE MUTATION BETA99 ASP-TYR STABILIZES Y-A NEW, COMPOSITE QUATERNARY STATE OF HUMAN HEMOGLOBIN
Overview
Carbonmonoxy hemoglobin Ypsilanti (beta 99 Asp-Tyr) exhibits a quaternary, form distinctly different from any structures previously observed for, human hemoglobins. The relative orientation of alpha beta dimers in the, new quaternary form lies well outside the range of values observed for, normal unliganded and liganded tetramers (Baldwin, J., Chothia, C., J., Mol. Biol. 129:175-220, 1979). Despite this large quaternary structural, difference between carbonmonoxy hemoglobin Ypsilanti and the two canonical, structures, the new quaternary structure's hydrogen bonding interactions, in the "switch" region, and packing interactions in the "flexible joint", region, show noncovalent interactions characteristic of the alpha 1 beta 2, contacts of both unliganded and liganded normal hemoglobins. In contrast, to both canonical structures, the beta 97 histidine residue in, carbonmonoxy hemoglobin Ypsilanti is disengaged from quaternary packing, interactions that are generally believed to enforce two-state behavior in, ligand binding. These features of the new quaternary structure, denoted Y, may therefore be representative of quaternary states that occur, transiently along pathways between the normal unliganded, T, and liganded, R, hemoglobin structures.
About this Structure
1CMY is a Protein complex structure of sequences from Homo sapiens with HEM as ligand. Full crystallographic information is available from OCA.
Reference
The mutation beta 99 Asp-Tyr stabilizes Y--a new, composite quaternary state of human hemoglobin., Smith FR, Lattman EE, Carter CW Jr, Proteins. 1991;10(2):81-91. PMID:1896430
Page seeded by OCA on Thu Nov 8 12:59:20 2007
