Journal
CHEMBIOCHEM
Volume 13, Issue 10, Pages 1393-1399Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201200189
Keywords
G protein-coupled receptors; molecular modeling; sequence alignment; structure elucidation
Funding
- MICINN [SAF2010-22198-C02-02]
- ISCIII [RD07/0067/0008]
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Comparison of the crystal structures of G protein-coupled receptors (GPCRs) revealed backbone irregularities in the majority of the transmembrane (TM) helices. Among these, wide (p bulge) and tight (310) helical turns on TM2 and TM5 deserve special attention because of their proximity to the ligand binding site. These irregularities are related to residue insertion or deletion (reflected by inclusion of gaps in sequence alignments) accumulated during the evolution of these two helices. These findings have direct implications for the sequence alignments, phylogeny reconstruction, and homology modeling of class A GPCRs.
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