1nih: Difference between revisions
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|PDB= 1nih |SIZE=350|CAPTION= <scene name='initialview01'>1nih</scene>, resolution 2.6Å | |PDB= 1nih |SIZE=350|CAPTION= <scene name='initialview01'>1nih</scene>, resolution 2.6Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HNI:PROTOPORPHYRIN+IX+CONTAINING+NI(II)'>HNI</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nih OCA], [http://www.ebi.ac.uk/pdbsum/1nih PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nih RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
We have determined the structure of a T-state haemoglobin in which the haem groups of the beta subunits have carbon monoxide bound, and the alpha subunits have nickel replacing the haem iron and are ligand-free. The structural adjustments on binding ligand in the T state are in the same direction as those associated with the quaternary transition, and a translational shift of the haem is severely restricted. We explain how these observations may account for the low ligand affinity of the beta haem of T-state haemoglobin. | We have determined the structure of a T-state haemoglobin in which the haem groups of the beta subunits have carbon monoxide bound, and the alpha subunits have nickel replacing the haem iron and are ligand-free. The structural adjustments on binding ligand in the T state are in the same direction as those associated with the quaternary transition, and a translational shift of the haem is severely restricted. We explain how these observations may account for the low ligand affinity of the beta haem of T-state haemoglobin. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Liddington, B.]] | [[Category: Liddington, B.]] | ||
[[Category: Luisi, B.]] | [[Category: Luisi, B.]] | ||
[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:30:51 2008'' | ||
Revision as of 19:30, 30 March 2008
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| 1nih, resolution 2.6Å | |||||||||||||
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| Ligands: | CMO, HEM, HNI, IHP | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Structure of deoxy-quaternary haemoglobin with liganded beta subunits
Overview
We have determined the structure of a T-state haemoglobin in which the haem groups of the beta subunits have carbon monoxide bound, and the alpha subunits have nickel replacing the haem iron and are ligand-free. The structural adjustments on binding ligand in the T state are in the same direction as those associated with the quaternary transition, and a translational shift of the haem is severely restricted. We explain how these observations may account for the low ligand affinity of the beta haem of T-state haemoglobin.
About this Structure
1NIH is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of deoxy-quaternary haemoglobin with liganded beta subunits., Luisi B, Liddington B, Fermi G, Shibayama N, J Mol Biol. 1990 Jul 5;214(1):7-14. PMID:2370669
Page seeded by OCA on Sun Mar 30 22:30:51 2008
