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Structural models for dimerization of G‐protein coupled receptors: The opioid receptor homodimers
Author(s) -
Filizola Marta,
Weinstein Harel
Publication year - 2002
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10311
Subject(s) - g protein coupled receptor , receptor , chemistry , computational biology , transmembrane domain , transmembrane protein , opioid receptor , biophysics , opioid , biochemistry , biology
Abstract Among the most exciting functional features of G‐protein coupled receptors (GPCRs) that are coming into focus lately are those relating to the role and structural characteristics of their oligomerization (mostly homo‐ and heterodimers). The structural underpinnings of these novel functional insights are still not clear, as current experimental techniques have not yet succeeded in identifying the dimerization interfaces between GPCR monomers. Two computational approaches have recently been designed in our lab to provide reasonable three‐dimensional (3D) molecular models of the transmembrane (TM) regions of GPCR dimers based on a combination of the structural information of receptor monomers and analyses of correlated mutations in receptor families. The modeling of GPCR heterodimers has been described recently. We present here a related approach for modeling of GPCR homodimers that identifies the interfaces in the most likely configurations of the complexes. The approach is illustrated for the three cloned opioid receptor subtypes (OPRD, OPRM, and OPRK). © 2002 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 66:317–325, 2002