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Publication Abstract from PubMed

Our aim is to shed light on the conservation of potential ligand docking sites that play an important role in ligand dynamics of globins by using the technique of filling with xenon atoms internal cavities, naturally present in hemoglobin and myoglobin. In particular, we present the high resolution structures of the Xe-adduct of deoxygenated wild type human hemoglobin and a quadruple mutant (L(B10)Y and H(E7)Q in alpha and beta chains). For the sake of comparison we also determined under the same experimental conditions the xenon complex of wild type sperm whale myoglobin.The analysis revealed that the number and position of Xe binding cavities is different in the alpha and beta subunits, the latter being more similar to myoglobin. Notably no proximal Xe docking site was detected in hemoglobin, at variance with myoglobin. The pattern of internal cavities accessibility and affinity for xenon suggests a different role for the dynamics of ligand migration in the two types of hemoglobin chains as compared to myoglobin. The number and position of hydrophobic cavities in hemoglobin is briefly discussed also in comparison with the data available for other members of the globin superfamily. (c) 2009 Wiley Periodicals, Inc. Biopolymers, 2009.

Pattern of cavities in globins: The case of human hemoglobin.,Savino C, Miele AE, Draghi F, Johnson KA, Sciara G, Brunori M, Vallone B Biopolymers. 2009 Apr 13. PMID:19365817^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.