1xz2

From Proteopedia

Revision as of 18:06, 12 November 2007

wild-type hemoglobin deoxy no-salt

Overview

Previous mutational studies on Tyr42alpha variants as well as the current, studies on the mutant hemoglobin alphaY42A show that the intersubunit, interactions associated with Tyr42alpha significantly stabilize the, alpha1beta2 interface of the quaternary-T deoxyhemoglobin tetramer., However, crystallographic studies, UV and visible resonance Raman, spectroscopy, CO combination kinetic measurements, and oxygen binding, measurements on alphaY42A show that the intersubunit interactions formed, by Tyr42alpha have only a modest influence on the structural properties, and ligand affinity of the deoxyhemoglobin tetramer. Therefore, the, alpha1beta2 interface interactions associated with Tyr42alpha do not, contribute significantly to the quaternary constraints that are, responsible for the low oxygen affinity of deoxyhemoglobin. The slight, increase in the ligand affinity of deoxy alphaY42A correlates with small, mutation-induced structural changes that perturb the environment of, Trp37beta, a critical region of the quaternary-T alpha1beta2 interface, that has been shown to be the major source of quaternary constraint in, deoxyhemoglobin.

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

1XZ2 is a Protein complex structure of sequences from Homo sapiens with HEM as ligand. Full crystallographic information is available from OCA.

Reference

Intersubunit interactions associated with Tyr42 alpha stabilize the quaternary-T tetramer but are not major quaternary constraints in deoxyhemoglobin., Kavanaugh JS, Rogers PH, Arnone A, Hui HL, Wierzba A, DeYoung A, Kwiatkowski LD, Noble RW, Juszczak LJ, Peterson ES, Friedman JM, Biochemistry. 2005 Mar 15;44(10):3806-20. PMID:15751957

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