Wide turn diversity in protein transmembrane helices implications for G-protein-coupled receptor and other polytopic membrane protein structure and function

Molecular Pharmacology
R Peter RiekRobert M Graham

Abstract

Previously, we showed that perturbations of protein transmembrane helices are manifested as one of three types of noncanonical structures (wide turns, tight turns, and kinks), which, compared with alpha-helices, are evident by distinctive Calpha(i)-->Calpha(x) distances. In this study, we report the analysis of more than 3000 transmembrane helices in 244 crystal structures from which we identified 70 wide turns (29 proline- and 41 nonproline-induced). Based on differences in the Calpha(i)-->Calpha(i)(-4) and Calpha(i)-->Calpha(i)(-5) profiles, we show that wide turns can be subclassified into three distinct subclasses (W(1), W(2), and W(3)) that differ with regard to the number and position of backbone i --> i-5 H-bonds formed N-terminal to the perturbing or signature proline or nonproline residue. Although wide turns generally produce changes in helical direction of 20 degrees to 30 degrees and a lateral shift in the helical axis, some of the W(3) subclass are associated with changes of <5 degrees . We also show that the distinct architectural features of wide turns allow the carbonyl bond of the i-4th residue, which is located on the widened loop of a wide turn, to be directed away from the helical axis. This provides regions...Continue Reading

References

Jun 5, 1988·Journal of Molecular Biology·D J Barlow, J M Thornton
Dec 1, 1995·Proteins·D Frishman, P Argos
Apr 4, 1997·Science·K R MacKenzieD M Engelman
Jun 1, 1997·Computer Applications in the Biosciences : CABIOS·G LabesseJ P Mornon
Aug 1, 1997·Protein Science : a Publication of the Protein Society·R L Dunbrack, F E Cohen
Dec 11, 1999·Nucleic Acids Research·H M BermanP E Bourne
Mar 15, 2000·Journal of Molecular Biology·W P Russ, D M Engelman
Mar 30, 2000·Protein Science : a Publication of the Protein Society·T M Weaver
May 8, 2000·Journal of Biomolecular Structure & Dynamics·M BansalR Velavan
Oct 31, 2000·Protein Engineering·I VisiersH Weinstein
Jan 21, 2001·The Journal of Biological Chemistry·S ScheinerY Gu
Mar 10, 2001·Journal of Molecular Biology·R P RiekR M Graham
Aug 2, 2001·Proceedings of the National Academy of Sciences of the United States of America·A SenesD M Engelman
May 30, 2002·Protein Engineering·M N Fodje, Salam Al-Karadaghi
Nov 6, 2002·Journal of Molecular Biology·Frank S CordesMark S P Sansom
Jan 31, 2003·Proteins·Simon C LovellDavid C Richardson
Dec 16, 2003·Proceedings of the National Academy of Sciences of the United States of America·Tomitake TsukiharaShinya Yoshikawa
Jan 17, 2004·Structure·Jean-Philippe Cartailler, Hartmut Luecke
Aug 18, 2004·Current Opinion in Structural Biology·Alessandro SenesWilliam F DeGrado
Dec 15, 2004·Journal of Molecular Modeling·Pranab K MohapatraMukesh K Raval
Jan 27, 2005·Journal of Molecular Graphics & Modelling·Jaime Arce LoperaJean-Pierre Duneau
Sep 24, 2005·Proceedings of the National Academy of Sciences of the United States of America·Sanguk KimJames U Bowie
Aug 16, 2006·Proceedings of the National Academy of Sciences of the United States of America·Hitoshi Nakamichi, Tetsuji Okada
Dec 13, 2006·FEBS Letters·Richard B TunnicliffeMike P Williamson
May 2, 2007·Proceedings of the National Academy of Sciences of the United States of America·Kazumasa MuramotoShinya Yoshikawa

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Citations

Dec 26, 2015·Journal of Chemical Information and Modeling·Norbert JeszenőiCsaba Hetényi
Dec 19, 2012·Trends in Pharmacological Sciences·Edward C Hulme
Sep 11, 2010·Journal of Structural Biology·R Peter Riek, Robert M Graham
May 12, 2010·Journal of Structural Biology·Julien ReyMarie Chabbert
Oct 25, 2011·Channels·Gregory M LipkindDorothy A Hanck
Jul 5, 2012·Chembiochem : a European Journal of Chemical Biology·Angel GonzalezLeonardo Pardo
May 14, 2009·Biopolymers·Jaime ArceJean-Pierre Duneau

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