{"title":"Chemotaxis receptors and signaling.","authors":"Aaron F Miller, Joseph J Falke","doi":"10.1016/S0065-3233(04)68011-9","DOIUrl":null,"url":null,"abstract":"<p><p>Chemotaxis is an important cellular response common in biology. In many chemotaxing cells the signal that regulates movement is initiated by G protein-coupled receptors on the cell surface that bind specific chemoattractants. These receptors share important structural similarities with other G protein-coupled receptors, including rhodopsin, which currently serves as the best starting point for modeling their structures. However, the chemotaxis receptors also share a number of relatively unique structural features that are less common in other GPCRs. The chemoattractant ligands of chemotaxis receptors exhibit a broad variety of sizes and chemical properties, ranging from small molecules and peptides to protein ligands. As a result, different chemotaxis receptors have evolved specialized mechanisms for the early steps of ligand binding and receptor activation. The mechanism of transmembrane signaling is currently under intensive study and several alternate mechanisms proposing different conformational rearrangements of the transmembrane helices have been proposed. Some chemotaxis receptors are proposed to form dimers, and in certain cases dimer formation is proposed to play a role in transmembrane signaling. In principle the structural and dynamical changes that occur during transmembrane signaling could be specialized for different receptors, or could be broadly conserved. Extensive mutagenesis studies have been carried out, and have begun to identify critical residues involved in ligand binding, receptor activation, and transmembrane signaling.</p>","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"68 ","pages":"393-444"},"PeriodicalIF":0.0000,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-3233(04)68011-9","citationCount":"33","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Advances in Protein Chemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1016/S0065-3233(04)68011-9","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 33
Abstract
Chemotaxis is an important cellular response common in biology. In many chemotaxing cells the signal that regulates movement is initiated by G protein-coupled receptors on the cell surface that bind specific chemoattractants. These receptors share important structural similarities with other G protein-coupled receptors, including rhodopsin, which currently serves as the best starting point for modeling their structures. However, the chemotaxis receptors also share a number of relatively unique structural features that are less common in other GPCRs. The chemoattractant ligands of chemotaxis receptors exhibit a broad variety of sizes and chemical properties, ranging from small molecules and peptides to protein ligands. As a result, different chemotaxis receptors have evolved specialized mechanisms for the early steps of ligand binding and receptor activation. The mechanism of transmembrane signaling is currently under intensive study and several alternate mechanisms proposing different conformational rearrangements of the transmembrane helices have been proposed. Some chemotaxis receptors are proposed to form dimers, and in certain cases dimer formation is proposed to play a role in transmembrane signaling. In principle the structural and dynamical changes that occur during transmembrane signaling could be specialized for different receptors, or could be broadly conserved. Extensive mutagenesis studies have been carried out, and have begun to identify critical residues involved in ligand binding, receptor activation, and transmembrane signaling.