TAILIEUCHUNG - Báo cáo khoa học: Human haptoglobin structure and function – a molecular modelling study

Hemoglobin is the most prominent protein in blood, transporting O2 and facilitating reactive oxygen and nitrogen species detoxification. Hemoglobin metabolism leads to the release of extra-erythrocytic hemoglobin, with potentially severe consequences for health. Extra-erythrocytic hemoglobin is complexed to haptoglobin for clearance by tissue macrophages. | ễFEBS Journal Human haptoglobin structure and function - a molecular modelling study F. Polticelli1 A. Bocedi1 G. Minervini1 and P. Ascenzi1 2 1 Department of Biology and InterdepartmentalLaboratory for Electron Microscopy University Roma Tre Italy 2 NationalInstitute for Infectious Diseases . Lazzaro Spallanzani Rome Italy Keywords chaperone-like activity covalent multimers haemoglobin haptoglobin homology modelling Correspondence F. Polticelli Department of Biology University Roma Tre Viale Guglielmo Marconi 446 I-00146 Rome Italy Fax 39 06 57336321 Tel 39 06 57336362 E-mail polticel@ Database Models data are available in the Protein Model DataBase under the accession numbers PM0075388 and PM0075389 Received 8 July 2008 revised 11 September 2008 accepted 17 September 2008 doi Hemoglobin is the most prominent protein in blood transporting O2 and facilitating reactive oxygen and nitrogen species detoxification. Hemoglobin metabolism leads to the release of extra-erythrocytic hemoglobin with potentially severe consequences for health. Extra-erythrocytic hemoglobin is complexed to haptoglobin for clearance by tissue macrophages. The human gene for haptoglobin consists of three structural alleles Hp1F Hp1S and Hp2. The products of the Hp1F and Hp1S alleles differ by only one amino acid whereas the Hp2 allele is the result of a fusion of the Hp1F and Hp1S alleles is present only in humans and gives rise to a longer a-chain. Haptoglobin consists of a dimer of ab-chains covalently linked by a disulphide bond between the Cys15 residue of each a-chain. However the presence of the Hp1 and Hp2 alleles in humans gives rise to HPT1-1 dimers covalently linked by Cys15 residues HPT1-2 heterooligomers and HPT2-2 oligomers. In fact the HPT2 variant displays two free Cys residues Cys15 and Cys74 whose participation in intermolecular disulphide bonds gives rise to higher-order covalent multimers. Here the complete modelling of .

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