LEADER 04626nam 22006015 450 001 9910337938403321 005 20200703171032.0 010 $a3-030-14265-5 024 7 $a10.1007/978-3-030-14265-0 035 $a(CKB)4100000008217399 035 $a(MiAaPQ)EBC5776031 035 $a(DE-He213)978-3-030-14265-0 035 $a(PPN)236519867 035 $a(EXLCZ)994100000008217399 100 $a20190516d2019 u| 0 101 0 $aeng 135 $aurcnu|||||||| 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aDirect Mechanisms in Cholesterol Modulation of Protein Function /$fedited by Avia Rosenhouse-Dantsker, Anna N. Bukiya 205 $a1st ed. 2019. 210 1$aCham :$cSpringer International Publishing :$cImprint: Springer,$d2019. 215 $a1 online resource (179 pages) 225 1 $aAdvances in Experimental Medicine and Biology,$x0065-2598 ;$v1135 311 $a3-030-14264-7 327 $aIntroduction -- Direct binding of cholesterol to proteins -- Cholesterol-recognition motifs in membrane proteins -- Molecular determinants of cholesterol binding to proteins: overview of crystallographic studies -- Crystallographic studies of steroid-protein interactions -- Insights into cholesterol binding sites in proteins from computational studies -- Cholesterol binding to NPC1/NPC2 -- I Biophysical elements of the interaction between cholesterol and the nicotinic acetylcholine receptor -- Modulation of TRPV1 channels by cholesterol -- Cholesterol binding sites in inwardly rectifying potassium channels. 330 $aIn this book, renowned scientists describe how cholesterol interacts with various proteins. Recent progress made in the high-resolution visualization of cholesterol-protein interactions using crystallography and cryogenic electron microscopy has substantially advanced the knowledge of critical features. These features enable specific recognition of the cholesterol molecule by proteins, a process that was built on earlier studies using binding assays, computational modeling and site-directed mutagenesis. Direct Mechanisms in Cholesterol Modulation of Protein Function offers comprehensive insights into the current understanding of cholesterol-driven modulation of protein function via direct sensing. Its nine chapters are organized into two distinct parts. In the first part, the chapters introduce the reader to the general characteristics of cholesterol binding sites in proteins. This part starts with a tour into common cholesterol recognition motifs, followed by an overview of the major classes of steroid-binding proteins. It then continues with two chapters that present a comprehensive analysis of molecular and structural characteristics of cholesterol binding sites in transmembrane and soluble protein domains. In the second part of the book, examples of cholesterol binding sites and consequences of specific cholesterol recognition for protein function are presented for G protein-coupled receptors, ion channels and cholesterol-transporting proteins. The book is valuable for undergraduate and graduate students in biochemistry and nutrition, as well as basic science and medical researchers with a keen interest in the biophysical properties of cholesterol and physiological consequences of cholesterol presence in biological systems. 410 0$aAdvances in Experimental Medicine and Biology,$x0065-2598 ;$v1135 606 $aProteomics 606 $aProteins  606 $aCell membranes  606 $aMolecular biology 606 $aProteomics$3https://scigraph.springernature.com/ontologies/product-market-codes/L1403X 606 $aProtein Science$3https://scigraph.springernature.com/ontologies/product-market-codes/L14040 606 $aMembrane Biology$3https://scigraph.springernature.com/ontologies/product-market-codes/L16050 606 $aMolecular Medicine$3https://scigraph.springernature.com/ontologies/product-market-codes/B1700X 615 0$aProteomics. 615 0$aProteins . 615 0$aCell membranes . 615 0$aMolecular biology. 615 14$aProteomics. 615 24$aProtein Science. 615 24$aMembrane Biology. 615 24$aMolecular Medicine. 676 $a612.0153 676 $a572.5795 702 $aRosenhouse-Dantsker$b Avia$4edt$4http://id.loc.gov/vocabulary/relators/edt 702 $aBukiya$b Anna N$4edt$4http://id.loc.gov/vocabulary/relators/edt 906 $aBOOK 912 $a9910337938403321 996 $aDirect Mechanisms in Cholesterol Modulation of Protein Function$91959939 997 $aUNINA