Bioactive conformation
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 toanymoleculeinabiologicallyrelevantboun…
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- Full title :Bioactive conformation / vol. ed.: Thomas Peters; with contrib. by S.V. Evans...[et al.].
Summary
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.
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- Publication Date:cop. 2007.
Publication Statements
- Publisher(s):Springer
- Place of Publication:Berlin [etc.]
- Language:eng
- Publication Date:cop. 2007.
The Physical Object
- Description:X, 309 p. : : ill. ; : 24 cm.
Edition Identifiers
- ISBN:3540490779, 9783540490777
- oclc:ocn774686082
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