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Titolo:
The structural and functional analysis of the hemoglobin D component from chicken
Autore:
Knapp, JE; Oliveira, MA; Xie, Q; Ernst, SR; Riggs, AF; Hackert, ML;
Indirizzi:
Univ Texas, Dept Chem & Biochem, Austin, TX 78712 USA Univ Texas Austin TX USA 78712 Dept Chem & Biochem, Austin, TX 78712 USA Univ Texas, Dept Zool, Austin, TX 78712 USA Univ Texas Austin TX USA 78712 niv Texas, Dept Zool, Austin, TX 78712 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 10, volume: 274, anno: 1999,
pagine: 6411 - 6420
SICI:
0021-9258(19990305)274:10<6411:TSAFAO>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-STRUCTURE REFINEMENT; OXYGEN-AFFINITY; CRYSTAL-STRUCTURE; HUMAN DEOXYHEMOGLOBIN; ORGANIC-PHOSPHATES; AREA DETECTOR; BLOOD; RESOLUTION; BINDING; ASSOCIATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
74
Recensione:
Indirizzi per estratti:
Indirizzo: Hackert, ML Univ Texas, Dept Chem & Biochem, Austin, TX 78712 USA Univ Texas Austin TX USA 78712 Biochem, Austin, TX 78712 USA
Citazione:
J.E. Knapp et al., "The structural and functional analysis of the hemoglobin D component from chicken", J BIOL CHEM, 274(10), 1999, pp. 6411-6420

Abstract

Oxygen binding by chicken blood shows enhanced cooperativity at high levels of oxygen saturation. This implies that deoxy hemoglobin tetramers self-associate. The crystal structure of an R-state form of chicken hemoglobin D has been solved to 2.3-Angstrom resolution using molecular replacement phases derived from human oxyhemoglobin. The model consists of an alpha(2)beta(2) tetramer in the asymmetric unit and has been refined to a R-factor of 0.222 (R-free = 0.257) for 29,702 reflections between 10,0- and 2.3-Angstrom resolution. Chicken Hb D differs most from human oxyhemoglobin in the AB and GH corners of the alpha subunits and the EF corner of the beta subunits, Reanalysis of published oxygen binding data for chicken Hbs shows that bothchicken Hb A and Hb D possess enhanced cooperativity in vitro when inositol hexaphosphate is present. The electrostatic surface potential for a calculated model of chicken deoxy-Hb D tetramers shows a pronounced hydrophobic patch that involves parts of the D and E helices of the beta subunits, Thishydrophobic patch is a promising candidate for a tetramer-tetramer interface that could regulate oxygen binding via the distal histidine.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 13:01:48