Structural insight into G-protein coupled receptor binding by apelin

Biochemistry
David N LangelaanJan K Rainey

Abstract

Apelin peptides are the cognate ligands for the G-protein coupled receptor APJ, with functions in the cardiovascular and central nervous systems, in glucose metabolism and as a human immunodeficiency virus (HIV-1) coreceptor. Apelin is found in 13-36 residue forms in vivo. The structures of five isoforms of apelin at physiological versus low (5-6 degrees C) temperature are compared here using circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy, demonstrating increased structure at low temperature. Far-ultraviolet (UV) CD spectra are predominantly random coil for apelin isoforms, but are convoluted by unusual bands from the C-terminal phenylalanine side chain. These bands, assigned using F13A-apelin-13, are accentuated at 5 degrees C and imply conformational restriction. At 35 degrees C, the R6-L9 region of apelin-17 is well structured, consistent with previous mutagenesis results showing necessity of this segment for apelin-APJ binding and activation. At 5 degrees C, R6-L9 retains its structuring while the functionally critical C-terminal G13-F17 region also becomes highly structured. Type IV beta-turns and some polyproline-II structure alongside F17 side chain motional reduction correlate well with CD spe...Continue Reading

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May 11, 2010·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·David N Langelaan, Jan K Rainey
Apr 2, 2011·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·David N LangelaanJan K Rainey
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Aug 28, 2009·The Journal of Physical Chemistry. B·David N Langelaan, Jan K Rainey

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