6hbw
From Proteopedia
|
Crystal structure of deoxy-human hemoglobin beta6 glu->trp
Overview
An atomic-level understanding of the interactions between hemoglobin, molecules that contribute to the formation of pathological fibers in, sickle cell disease remains elusive. By exploring crystal structures of, mutant hemoglobins with altered polymerization properties, insight can be, gained into sickle cell hemoglobin (HbS) polymerization. We present here, the 2.0-A resolution deoxy crystal structure of human hemoglobin mutated, to tryptophan at the beta6 position, the site of the glutamate --> valine, mutation in HbS. Unlike leucine and isoleucine, which promote, polymerization relative to HbS, tryptophan inhibits polymerization. Our, results provide explanations for the altered polymerization properties and, reveal a fundamentally different double strand that may provide a model, for interactions within a fiber and/or interactions leading to, heterogeneous nucleation.
About this Structure
6HBW is a Protein complex structure of sequences from Homo sapiens with HEM as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of deoxy-human hemoglobin beta6 Glu --> Trp. Implications for the structure and formation of the sickle cell fiber., Harrington DJ, Adachi K, Royer WE Jr, J Biol Chem. 1998 Dec 4;273(49):32690-6. PMID:9830011
Page seeded by OCA on Thu Nov 8 13:34:57 2007
