1b86

From Proteopedia

Revision as of 14:00, 12 November 2007

HUMAN DEOXYHAEMOGLOBIN-2,3-DIPHOSPHOGLYCERATE COMPLEX

Overview

The haemoglobin-2,3-diphosphoglycerate complex structure has been solved, at 2.5 A resolution using crystals grown from low-salt solutions. The, results show some important differences with the precedent, haemoglobin-2,3-diphosphoglycerate high-salt structure solved by Arnone., First, we observe a loss of symmetry in the binding site, secondly both of, the lysine residues 82 beta interact with 2,3-diphosphoglycerate at the, same time, each making two contacts. This level of interaction is in, agreement with the functional behaviour of natural haemoglobin mutants, with mutations at the 2,3-diphosphoglycerate binding site.

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

1B86 is a Protein complex structure of sequences from Homo sapiens with DDH, HEM and DG2 as ligands. Full crystallographic information is available from OCA.

Reference

Human deoxyhaemoglobin-2,3-diphosphoglycerate complex low-salt structure at 2.5 A resolution., Richard V, Dodson GG, Mauguen Y, J Mol Biol. 1993 Sep 20;233(2):270-4. PMID:8377203

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