1hac
From Proteopedia
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CROSSLINKED HAEMOGLOBIN
Contents |
Overview
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.
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
1HAC is a Protein complex structure of sequences from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
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:9223274
Page seeded by OCA on Thu Feb 21 12:59:13 2008
Categories: Homo sapiens | Protein complex | Brennan, R G. | Dixon, M M. | Jones, R T. | Kluger, R. | Schumacher, M A. | CMO | HEM | NDD | Erythrocyte | Heme | Oxygen transport | Respiratory protein
