1gzx

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[[Image:1gzx.gif|left|200px]]
[[Image:1gzx.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1gzx |SIZE=350|CAPTION= <scene name='initialview01'>1gzx</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1gzx", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=HB1:O2+Binding+Site+For+Chain+D'>HB1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1gzx| PDB=1gzx | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gzx OCA], [http://www.ebi.ac.uk/pdbsum/1gzx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gzx RCSB]</span>
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}}
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'''OXY T STATE HAEMOGLOBIN: OXYGEN BOUND AT ALL FOUR HAEMS'''
'''OXY T STATE HAEMOGLOBIN: OXYGEN BOUND AT ALL FOUR HAEMS'''
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[[Category: Tame, J.]]
[[Category: Tame, J.]]
[[Category: Wilkinson, A.]]
[[Category: Wilkinson, A.]]
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[[Category: cooperativity]]
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[[Category: Cooperativity]]
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[[Category: haem protein]]
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[[Category: Haem protein]]
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[[Category: oxygen binding]]
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[[Category: Oxygen binding]]
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[[Category: transport]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:14:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:54:54 2008''
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Revision as of 15:14, 2 May 2008

Template:STRUCTURE 1gzx

OXY T STATE HAEMOGLOBIN: OXYGEN BOUND AT ALL FOUR HAEMS


Overview

The cooperative binding of oxygen by haemoglobin results from restraints on ligand binding in the T state. The unfavourable interactions made by the ligands at the haems destabilise the T state and favour the high affinity R state. The T <==> R equilibrium leads, in the presence of a ligand, to a rapid increase in the R state population and therefore generates cooperative binding. There is now considerable understanding of this phenomenon, but the interactions that reduce ligand affinity in the T state have not yet been fully explored, owing to the difficulties in preparing T state haemoglobin crystals in which all the subunits are oxygenated. A protocol has been developed to oxygenate deoxy T state adult human haemoglobin (HbA) crystals in air at 4 C at all four haems without significant loss of crystalline order. The X-ray crystal structure, determined to 2.1 A spacing, shows significant changes in the alpha and beta haem pockets as well as changes at the alpha(1)beta(2) interface in the direction of the R quaternary structure. Most of the shifts and deviations from deoxy T state HbA are similar to, but larger than, those previously observed in the T state met and other partially liganded T state forms. They provide clear evidence of haem-haem interaction in the T state.

About this Structure

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

Reference

Crystal structure of T state haemoglobin with oxygen bound at all four haems., Paoli M, Liddington R, Tame J, Wilkinson A, Dodson G, J Mol Biol. 1996 Mar 8;256(4):775-92. PMID:8642597 Page seeded by OCA on Fri May 2 18:14:04 2008

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