2hhd

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{{STRUCTURE_2hhd| PDB=2hhd | SCENE= }}
{{STRUCTURE_2hhd| PDB=2hhd | SCENE= }}
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'''OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF THE BETA-CHAINS IN HUMAN AND BOVINE HEMOGLOBIN'''
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===OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF THE BETA-CHAINS IN HUMAN AND BOVINE HEMOGLOBIN===
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==Overview==
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The crystal structure of the mutant deoxyhemoglobin in which the beta-globin Val67(E11) has been replaced with threonine [Fronticelli et al. (1993) Biochemistry 32, 1235-1242] has been determined at 2.2 A resolution. Prior to the crystal structure determination, molecular modeling indicated that the Thr67(E11) side chain hydroxyl group in the distal beta-heme pocket forms a hydrogen bond with the backbone carbonyl of His63(E7) and is within hydrogen-bonding distance of the N delta of His63(E7). The mutant crystal structure indicates only small changes in conformation in the vicinity of the E11 mutation confirming the molecular modeling predictions. Comparison of the structures of the mutant beta-subunits and recombinant porcine myoglobin with the identical mutation [Cameron et al. (1993) Biochemistry 32, 13061-13070] indicates similar conformations of residues in the distal heme pocket, but there is no water molecule associated with either of the threonines of the beta-subunits. The introduction of threonine into the distal heme pocket, despite having only small perturbations in the local structure, has a marked affect on the interaction with ligands. In the oxy derivative there is a 2-fold decrease in O2 affinity [Fronticelli et al. (1993) Biochemistry 32, 1235-1242], and the rate of autoxidation is increased by 2 orders of magnitude. In the CO derivative the IR spectrum shows modifications with respect to that of normal human hemoglobin, suggesting the presence of multiple CO conformers. In the nitrosyl derivative an interaction with the O gamma atom of Thr67(E11) is probably responsible for the 10-fold increase in the rate of NO release from the beta-subunits. In the aquomet derivative there is a 6-fold decrease in the rate of hemin dissociation suggesting an interaction of the Fe-coordinated water with the O gamma of Thr67(E11).
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{{ABSTRACT_PUBMED_8639677}}
==About this Structure==
==About this Structure==
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[[Category: Pechik, I.]]
[[Category: Pechik, I.]]
[[Category: Oxygen transport]]
[[Category: Oxygen transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:17:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat Jul 5 16:23:36 2008''

Revision as of 13:23, 5 July 2008

Image:2hhd.png


PDB ID 2hhd

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2hhd, resolution 2.20Å ()
Ligands: ,
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF THE BETA-CHAINS IN HUMAN AND BOVINE HEMOGLOBIN

Template:ABSTRACT PUBMED 8639677

About this Structure

2HHD is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystallographic, molecular modeling, and biophysical characterization of the valine beta 67 (E11)-->threonine variant of hemoglobin., Pechik I, Ji X, Fidelis K, Karavitis M, Moult J, Brinigar WS, Fronticelli C, Gilliland GL, Biochemistry. 1996 Feb 13;35(6):1935-45. PMID:8639677

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