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Titolo:
Structural organization of G-protein-coupled receptors
Autore:
Lomize, AL; Pogozheva, ID; Mosberg, HI;
Indirizzi:
Univ Michigan, Coll Pharm, Ann Arbor, MI 48109 USA Univ Michigan Ann Arbor MI USA 48109 Coll Pharm, Ann Arbor, MI 48109 USA
Titolo Testata:
JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN
fascicolo: 4, volume: 13, anno: 1999,
pagine: 325 - 353
SICI:
0920-654X(199907)13:4<325:SOOGR>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
SITE-DIRECTED MUTAGENESIS; BETA-ADRENERGIC-RECEPTOR; 2ND EXTRACELLULAR LOOP; DELTA-OPIOID RECEPTOR; MUSCARINIC ACETYLCHOLINE-RECEPTORS; MEMBRANE-SPANNING SEGMENT; ANGIOTENSIN-II RECEPTOR; DOPAMINE D2 RECEPTOR; AMINO-ACID-RESIDUES; BINDING-SITE;
Keywords:
distance geometry; H-bonding; membrane proteins; molecular modeling; protein structure;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
142
Recensione:
Indirizzi per estratti:
Indirizzo: Mosberg, HI Univ Michigan, Coll Pharm, Ann Arbor, MI 48109 USA Univ Michigan Ann Arbor MI USA 48109 Ann Arbor, MI 48109 USA
Citazione:
A.L. Lomize et al., "Structural organization of G-protein-coupled receptors", J COMPUT A, 13(4), 1999, pp. 325-353

Abstract

Atomic-resolution structures of the transmembrane 7-alpha-helical domains of 26 G-protein-coupled receptors (GPCRs) (including opsins, cationic amine, melatonin, purine, chemokine, opioid, and glycoprotein hormone receptors and two related proteins, retinochrome and Duffy erythrocyte antigen) were calculated by distance geometry using interhelical hydrogen bonds formed byvarious proteins from the family and collectively applied as distance constraints, as described previously [Pogozheva et al., Biophys. J., 70 (1997) 1963]. The main structural features of the calculated GPCR models are described and illustrated by examples. Some of the features reflect physical interactions that are responsible for the structural stability of the transmembrane alpha-bundle: the formation of extensive networks of interhelical H-bonds and sulfur-aromatic clusters that are spatially organized as 'polaritygradients'; the close packing of side-chains throughout the transmembrane domain; and the formation of interhelical disulfide bonds in some receptorsand a plausible Zn2+ binding center in retinochrome. Other features of themodels are related to biological function and evolution of GPCRs: the formation of a common 'minicore' of 43 evolutionarily conserved residues; a multitude of correlated replacements throughout the transmembrane domain; an Na+-binding site in some receptors, and excellent complementarity of receptor binding pockets to many structurally dissimilar, conformationally constrained ligands, such as retinal, cyclic opioid peptides, and cationic amine ligands. The calculated models are in good agreement with numerous experimental data.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/01/20 alle ore 06:51:12