1cmy: Difference between revisions

Revision as of 20:58, 30 June 2008

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File:1cmy.png

Template:STRUCTURE 1cmy

THE MUTATION BETA99 ASP-TYR STABILIZES Y-A NEW, COMPOSITE QUATERNARY STATE OF HUMAN HEMOGLOBINTHE MUTATION BETA99 ASP-TYR STABILIZES Y-A NEW, COMPOSITE QUATERNARY STATE OF HUMAN HEMOGLOBIN

Template:ABSTRACT PUBMED 1896430

About this StructureAbout this Structure

1CMY is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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

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-[[Image:1cmy.gif|left|200px]]
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-'''THE MUTATION BETA99 ASP-TYR STABILIZES Y-A NEW, COMPOSITE QUATERNARY STATE OF HUMAN HEMOGLOBIN'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_1896430}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 1896430 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_1896430}}
 ==About this Structure==
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 [[Category: Smith, F R.]]
 [[Category: Oxygen transport]]
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