1hac: Difference between revisions
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[[Image:1hac. | [[Image:1hac.jpg|left|200px]]<br /><applet load="1hac" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1hac" size=" | |||
caption="1hac, resolution 2.60Å" /> | caption="1hac, resolution 2.60Å" /> | ||
'''CROSSLINKED HAEMOGLOBIN'''<br /> | '''CROSSLINKED HAEMOGLOBIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1HAC 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 HEM, CMO and NDD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1HAC 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=HEM:'>HEM</scene>, <scene name='pdbligand=CMO:'>CMO</scene> and <scene name='pdbligand=NDD:'>NDD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HAC OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: respiratory protein]] | [[Category: respiratory protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:55:30 2008'' | ||
Revision as of 16:55, 15 February 2008
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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 with , and as ligands. 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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