Engineering and design of ligand-induced conformational change in proteins.
The ability to manipulate ligand-induced conformational change, although representing a major challenge to the protein engineer, is an essential end point in efforts to produce novel functional proteins for biotechnology and therapeutic applications. Progress towards this goal requires determining not only what factors control the fold and stability of a protein, but also how ligand binding alters the complex conformational/energetic landscape. Important strides are being made on several fronts, including understanding the origin of long-range effects and allosteric structural mechanisms, using both experimental and theoretical approaches.
Mizoue
Laura S
LS
Department of Biochemistry, Center for Structural Biology, 896 PRB, Vanderbilt University, Nashville, TN 37232-0146, USA. l.mizoue@vanderbilt.edu
Chazin
Walter J
WJ
D064026:Calbindins; D002147:Calmodulin / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry; D016023:Integrins / Q000737:chemistry; D008024:Ligands; D058619:Maltose-Binding Proteins; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D064030:S100 Calcium Binding Protein G / Q000737:chemistry
D064026:Calbindins; D002147:Calmodulin; D002352:Carrier Proteins; D016023:Integrins; D008024:Ligands; D058619:Maltose-Binding Proteins; D011506:Proteins; D064030:S100 Calcium Binding Protein G