Difference between restoring and predicting 3D structures of the loops in G-protein–coupled receptors by molecular modeling
Year: 2011
Type: letter
Abstract: Goldfeld et al. (1) presented modeling results on restoring 3D structures of the intra- and extracellular loops in bovine rhodopsin (bRh), human A2A adenosine receptor (A2Ar), turkey β1-adrenergic receptor (β1AR), and human β2-adrenergic receptor (β2AR). In all cases, the lowest energy conformers of the loops matched the corresponding X-ray structures with excellent rmsd values. The extracellular loops for the same receptors were modeled in our article previously (2) with the use of a much less sophisticated modeling procedure. Goldfeld et al. (1) emphasized substantially better accuracy of reproducing the X-ray structures of the loops, especially larger loops, in their study compared with ours. Although their restoration of the loops is impressive, we believe it is important to outline differences between the two modeling procedures (1, 2) that were not sufficiently distinguished by Goldfeld et al. (1).
Authors: Gregory V. Nikiforovich, Christina M. Taylor, Garland R. Marshall, Thomas J. Baranski
Institution: Washington University in St. Louis
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W2007148127