1nih
From Proteopedia
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| - | [[Image:1nih.gif|left|200px]]<br /> | + | [[Image:1nih.gif|left|200px]]<br /><applet load="1nih" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1nih, resolution 2.6Å" /> | caption="1nih, resolution 2.6Å" /> | ||
'''Structure of deoxy-quaternary haemoglobin with liganded beta subunits'''<br /> | '''Structure of deoxy-quaternary haemoglobin with liganded beta subunits'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NIH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with HNI, HEM, CMO and IHP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1NIH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HNI:'>HNI</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=CMO:'>CMO</scene> and <scene name='pdbligand=IHP:'>IHP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:29:06 2008'' |
Revision as of 14:29, 15 February 2008
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Structure of deoxy-quaternary haemoglobin with liganded beta subunits
Contents |
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.
Disease
Known diseases associated with this structure: Erythremias, alpha- OMIM:[141800], Erythremias, beta- OMIM:[141900], Erythrocytosis OMIM:[141850], HPFH, deletion type OMIM:[141900], Heinz body anemia OMIM:[141850], Heinz body anemias, alpha- OMIM:[141800], Heinz body anemias, beta- OMIM:[141900], Hemoglobin H disease OMIM:[141850], Hypochromic microcytic anemia OMIM:[141850], Methemoglobinemias, alpha- OMIM:[141800], Methemoglobinemias, beta- OMIM:[141900], Sickle cell anemia OMIM:[141900], Thalassemia, alpha- OMIM:[141850], Thalassemia-beta, dominant inclusion-body OMIM:[141900], Thalassemias, alpha- OMIM:[141800], Thalassemias, beta- OMIM:[141900]
About this Structure
1NIH is a Protein complex structure of sequences from Homo sapiens with , , and as ligands. 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 Fri Feb 15 16:29:06 2008
Categories: Homo sapiens | Protein complex | Liddington, B. | Luisi, B. | CMO | HEM | HNI | IHP | Oxygen transport
