Determining membrane protein structures: still a challenge!
Determination of structures and dynamics events of transmembrane proteins is important for the understanding of their function. Analysis of such events requires high-resolution 3D structures of the different conformations coupled with molecular dynamics analyses describing the conformational pathways. However, the solution of 3D structures of transmembrane proteins at atomic level remains a particular challenge for structural biochemists--the need for purified and functional transmembrane proteins causes a 'bottleneck'. There are various ways to obtain 3D structures: X-ray diffraction, electron microscopy, NMR and modelling; these methods are not used exclusively of each other, and the chosen combination depends on several criteria. Progress in this field will improve knowledge of ligand-induced activation and inhibition of membrane proteins in addition to aiding the design of membrane-protein-targeted drugs.
Lacapère
Jean-Jacques
JJ
INSERM, U773, Centre de Recherche Biomédicale Bichat Beaujon CRB3, Faculté de Médecine X. Bichat, Université Paris 7, BP 416, F-75018, Paris, France. lacapere@bichat.inserm.fr
Pebay-Peyroula
Eva
E
Neumann
Jean-Michel
JM
Etchebest
Catherine
C
D018360:Crystallography, X-Ray; D015195:Drug Design; D008565:Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification; D008854:Microscopy, Electron; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation
D008565:Membrane Proteins