1hac: Difference between revisions
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[[Image:1hac.jpg|left|200px]] | [[Image:1hac.jpg|left|200px]] | ||
'''CROSSLINKED HAEMOGLOBIN''' | {{Structure | ||
|PDB= 1hac |SIZE=350|CAPTION= <scene name='initialview01'>1hac</scene>, resolution 2.60Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene> and <scene name='pdbligand=NDD:2,6-DICARBOXYNAPHTHALENE'>NDD</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CROSSLINKED HAEMOGLOBIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1HAC is a [ | 1HAC is a [[Protein complex]] structure of sequences 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=1HAC OCA]. | ||
==Reference== | ==Reference== | ||
Allosteric intermediates indicate R2 is the liganded hemoglobin end state., Schumacher MA, Zheleznova EE, Poundstone KS, Kluger R, Jones RT, Brennan RG, Proc Natl Acad Sci U S A. 1997 Jul 22;94(15):7841-4. PMID:[http:// | Allosteric intermediates indicate R2 is the liganded hemoglobin end state., Schumacher MA, Zheleznova EE, Poundstone KS, Kluger R, Jones RT, Brennan RG, Proc Natl Acad Sci U S A. 1997 Jul 22;94(15):7841-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9223274 9223274] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: respiratory protein]] | [[Category: respiratory protein]] | ||
''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 11:34:27 2008'' | ||
Revision as of 12:34, 20 March 2008
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| , resolution 2.60Å | |||||||
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| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CROSSLINKED HAEMOGLOBIN
OverviewOverview
Hemoglobin has been a long-standing paradigm for understanding protein allostery. Here, the x-ray structures of two chemically crosslinked, fully liganded hemoglobins, alpha2beta82CA82beta and alpha2beta82ND82beta, are described at 2.3 A and 2.6 A resolution, respectively. Strikingly, these crosslinked hemoglobins assume intermediate conformations that lie between those of R and the controversial liganded hemoglobin state R2 rather than between R and T. Thus, these structures support only a T left and right arrow R left and right arrow R2 allosteric pathway and underscore the physiological importance of the R2 conformation.
DiseaseDisease
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 StructureAbout this Structure
1HAC is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Allosteric intermediates indicate R2 is the liganded hemoglobin end state., Schumacher MA, Zheleznova EE, Poundstone KS, Kluger R, Jones RT, Brennan RG, Proc Natl Acad Sci U S A. 1997 Jul 22;94(15):7841-4. PMID:9223274
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