1xz2
From Proteopedia
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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.
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
Page seeded by OCA on Thu Nov 8 13:21:35 2007
