1cbl
From Proteopedia
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| - | [[Image:1cbl.jpg|left|200px]] | + | [[Image:1cbl.jpg|left|200px]] |
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| - | '''THE 1.9 ANGSTROM STRUCTURE OF DEOXY-BETA4 HEMOGLOBIN: ANALYSIS OF THE PARTITIONING OF QUATERNARY-ASSOCIATED AND LIGAND-INDUCED CHANGES IN TERTIARY STRUCTURE''' | + | {{Structure |
| + | |PDB= 1cbl |SIZE=350|CAPTION= <scene name='initialview01'>1cbl</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE 1.9 ANGSTROM STRUCTURE OF DEOXY-BETA4 HEMOGLOBIN: ANALYSIS OF THE PARTITIONING OF QUATERNARY-ASSOCIATED AND LIGAND-INDUCED CHANGES IN TERTIARY STRUCTURE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CBL is a [ | + | 1CBL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBL OCA]. |
==Reference== | ==Reference== | ||
| - | The 1.9 A structure of deoxy beta 4 hemoglobin. Analysis of the partitioning of quaternary-associated and ligand-induced changes in tertiary structure., Borgstahl GE, Rogers PH, Arnone A, J Mol Biol. 1994 Feb 25;236(3):831-43. PMID:[http:// | + | The 1.9 A structure of deoxy beta 4 hemoglobin. Analysis of the partitioning of quaternary-associated and ligand-induced changes in tertiary structure., Borgstahl GE, Rogers PH, Arnone A, J Mol Biol. 1994 Feb 25;236(3):831-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8114097 8114097] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:22:19 2008'' |
Revision as of 08:22, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE 1.9 ANGSTROM STRUCTURE OF DEOXY-BETA4 HEMOGLOBIN: ANALYSIS OF THE PARTITIONING OF QUATERNARY-ASSOCIATED AND LIGAND-INDUCED CHANGES IN TERTIARY STRUCTURE
Contents |
Overview
The crystal structure of the deoxygenated form of the human hemoglobin beta 4 tetramer (deoxy beta 4) has been determined and refined at a resolution of 1.9 A. A detailed comparison of the quaternary structures of carbonmonoxy-beta 4 (CO beta 4) and deoxy beta 4 shows that ligand binding to the beta 4 tetramer produces only slight movements of the subunits relative to each other. Therefore, unlike the hemoglobin alpha 2 beta 2 tetramer, where the transition from an unliganded T state tetramer to a liganded R state tetramer results in a large change in quaternary structure, beta 4 is locked in a quaternary structure that very closely resembles the R state. By comparing the high-resolution structures of T state deoxy alpha 2 beta 2, R state deoxy beta 4 and R state CO beta 4, it is possible to partition the changes in beta subunit tertiary structure into those that arise from changes in quaternary structure and those that result solely from ligand binding. Specifically, when viewed from the heme reference frame, comparison of the structures of T state deoxy alpha 2 beta 2 and R state deoxy beta 4 shows that the T-to-R quaternary structure transition induces changes in beta subunit tertiary structure that are approximately halfway toward the tertiary structure observed in liganded beta 4 and liganded alpha 2 beta 2. When viewed from the reference frame of the globin backbone atoms, the T-to-R quaternary structure transition induces a small rotation of the heme group and a shift of the "allosteric core" (the end of the F helix, the FG corner, the beginning of the G helix, and the heme group) away from the E helix. These movements open the ligand binding pocket and place the heme in a more symmetric position relative to the proximal histidine residue. Together, these effects work in unison to give the subunits of deoxy beta 4 a tertiary structure that has high ligand affinity.
Disease
Known diseases associated with this structure: Erythremias, beta- OMIM:[141900], HPFH, deletion type OMIM:[141900], Heinz body anemias, beta- OMIM:[141900], Methemoglobinemias, beta- OMIM:[141900], Sickle cell anemia OMIM:[141900], Thalassemia-beta, dominant inclusion-body OMIM:[141900], Thalassemias, beta- OMIM:[141900]
About this Structure
1CBL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The 1.9 A structure of deoxy beta 4 hemoglobin. Analysis of the partitioning of quaternary-associated and ligand-induced changes in tertiary structure., Borgstahl GE, Rogers PH, Arnone A, J Mol Biol. 1994 Feb 25;236(3):831-43. PMID:8114097
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