Bioactive Conformation I

Speci?c binding of a ligand to a receptor is a key step in a variety of biol- ical processes, such as immune reactions, enzyme cascades, or intracellular transport processes. The ligand receptor terminology implies that the rec- tor molecule is signi?cantly larger than the ligand, and the term bioac...

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Auteur principal : Peters Tom (Éditeur scientifique)
Format : Livre
Langue : anglais
Titre complet : Bioactive Conformation I / edited by Thomas Peters.
Édition : 1st ed. 2007.
Publié : Berlin, Heidelberg : Springer Berlin Heidelberg , [20..]
Cham : Springer Nature
Collection : Topics in current chemistry (Internet) ; 272
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Contenu : Spatial Screening for the Identification of the Bioactive Conformation of Integrin Ligands. Dynamics and Thermodynamics of Ligand Protein Interactions. The Fibroblast Growth Factor (FGF) FGF Receptor Complex: Progress Towards the Physiological State. Characterization of Interactions Between Misfolding Proteins and Molecular Chaperones by NMR Spectroscopy. NMR Analysis of Bioprotective Sugars: Sucrose and Oligomeric (1?2)-?-D-glucopyranosyl-(1?2)-?-D-fructofuranosides. Residual Dipolar Couplings Report on the Active Conformation of Rhodopsin-Bound Protein Fragments. Glycosyltransferase Structure and Function. Exploiting Ligand and Receptor Adaptability in Rational Drug Design Using Dynamics and Structure-Based Strategies
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Documents associés : Autre format: Bioactive conformation
Description
Résumé : Speci?c binding of a ligand to a receptor is a key step in a variety of biol- ical processes, such as immune reactions, enzyme cascades, or intracellular transport processes. The ligand receptor terminology implies that the rec- tor molecule is signi?cantly larger than the ligand, and the term bioactive conformation usually characterizes the conformation of a ligand when it is bound to a receptor. In a more general sense, bioactive conformation applies toanymoleculeinabiologicallyrelevantboundstateregardlessofsizecons- erations. Mostofthecontributions tothisbookaddressligandsthat aremuch smaller than their receptors. X-ray crystallography and high resolution NMR spectroscopy are the two main experimental techniques used to study bioactive conformations. The- fore,the twovolumes ofthisbookcover approachesthat use either ofthetwo techniques, or a combination thereof. The combination of X-ray crystallog- phy and NMR spectroscopy is particularly useful when a crystal structure of areceptorprotein,butnotofthereceptorprotein ligandcomplex,isavailable. Anumberofexperimentaltechniquestoanalyzethebioactiveconformationof aligandwithNMRarebasedontheobservationoftheresonancesignalsofthe free ligand that is in exchange with the bound ligand. Several chapters focus onsuchapproachesthat rangefrom classical transferredNOEexperiments, totransferreddipolarcouplings,toSTD(SaturationTransferDifference)NMR techniques. Incaseswhere tightbinding inthesub-nanomolar rangeprevents the analysis of the bioactive conformation via free ligand signals, the ligand protein complex has to be analyzed with protein NMR-based techniques or by crystallography. Since this area has been the subject of many reviews and monographs it will not be covered here in particular detail. As a unifying theme, all contributions target the question of how molecular recognition of biologically active molecules is achieved on the atomic scale
Variantes de titre : With contributions by numerous experts
ISBN : 978-3-540-49078-4
DOI : 10.1007/978-3-540-49078-4