1hbr: Difference between revisions

Revision as of 07:57, 1 July 2008

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File:1hbr.png

Template:STRUCTURE 1hbr

R-STATE FORM OF CHICKEN HEMOGLOBIN DR-STATE FORM OF CHICKEN HEMOGLOBIN D

Template:ABSTRACT PUBMED 10037733

About this StructureAbout this Structure

1HBR is a Protein complex structure of sequences from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

The structural and functional analysis of the hemoglobin D component from chicken., Knapp JE, Oliveira MA, Xie Q, Ernst SR, Riggs AF, Hackert ML, J Biol Chem. 1999 Mar 5;274(10):6411-20. PMID:10037733

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-'''R-STATE FORM OF CHICKEN HEMOGLOBIN D'''
+===R-STATE FORM OF CHICKEN HEMOGLOBIN D===
-==Overview==
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-Oxygen binding by chicken blood shows enhanced cooperativity at high levels of oxygen saturation. This implies that deoxy hemoglobin tetramers self-associate. The crystal structure of an R-state form of chicken hemoglobin D has been solved to 2.3-A resolution using molecular replacement phases derived from human oxyhemoglobin. The model consists of an alpha2 beta2 tetramer in the asymmetric unit and has been refined to a R-factor of 0.222 (R-free = 0.257) for 29,702 reflections between 10.0- and 2.3-A resolution. Chicken Hb D differs most from human oxyhemoglobin in the AB and GH corners of the alpha subunits and the EF corner of the beta subunits. Reanalysis of published oxygen binding data for chicken Hbs shows that both chicken Hb A and Hb D possess enhanced cooperativity in vitro when inositol hexaphosphate is present. The electrostatic surface potential for a calculated model of chicken deoxy-Hb D tetramers shows a pronounced hydrophobic patch that involves parts of the D and E helices of the beta subunits. This hydrophobic patch is a promising candidate for a tetramer-tetramer interface that could regulate oxygen binding via the distal histidine.
+The line below this paragraph, {{ABSTRACT_PUBMED_10037733}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: High cooperatiity]]
 [[Category: Oxygen transport]]
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