1hbs
From Proteopedia
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REFINED CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S. I. RESTRAINED LEAST-SQUARES REFINEMENT AT 3.0-ANGSTROMS RESOLUTION
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Overview
The crystal structure of deoxyhemoglobin S has been refined at 3.0-A, resolution using the Hendrickson-Konnert restrained least-squares method., Comparison with the structure of deoxyhemoglobin A reveals a hingelike, movement of the beta-chain A helices, which are involved in molecular, contacts, toward the EF corners of their respective subunits. This, movement brings the amino termini of the beta-chains closer to the, molecular dyad. The A helices remain alpha-helical throughout their entire, lengths. No other major structural difference is found between, deoxyhemoglobin A and deoxyhemoglobin S.
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
1HBS is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Refined crystal structure of deoxyhemoglobin S. I. Restrained least-squares refinement at 3.0-A resolution., Padlan EA, Love WE, J Biol Chem. 1985 Jul 15;260(14):8272-9. PMID:4008491
Page seeded by OCA on Fri Feb 15 15:55:45 2008
