NDLI: Probing protein conformational changes in living cells by using designer binding proteins: application to the estrogen receptor.

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Probing protein conformational changes in living cells by using designer binding proteins: application to the estrogen receptor.

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Probing protein conformational changes in living cells by using designer binding proteins: application to the estrogen receptor.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Koide, Akiko Abbatiello, Stacy Koide, Shohei Rothgery, Lisa
Description	Author Affiliation: Koide A ( Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, Rochester, NY 14642, USA.);
Abstract	A challenge in understanding the mechanism of protein function in biology is to establish the correlation between functional form in the intracellular environment and high-resolution structures obtained with in vitro techniques. Here we present a strategy to probe conformational changes of proteins inside cells. Our method involves: (i) engineering binding proteins to different conformations of a target protein, and (ii) using them to sense changes in the surface property of the target in cells. We probed ligand-induced conformational changes of the estrogen receptor alpha (ER alpha) ligand-binding domain (LBD). By using yeast two-hybrid techniques, we first performed combinatorial library screening of 'monobodies' (small antibody mimics using the scaffold of a fibronectin type III domain) for clones that bind to ER alpha and then characterized their interactions with ER alpha in the nucleus, the native environment of ER alpha, in the presence of various ligands. A library using a highly flexible loop yielded monobodies that specifically recognize a particular ligand complex of ER alpha, and the pattern of monobody specificity was consistent with the structural differences found in known crystal structures of ER alpha-LBD. A more restrained loop library yielded clones that bind both agonist- and antagonist-bound ER alpha. Furthermore, we found that a deletion of the ER alpha F domain that is C-terminally adjacent to the LBD increased the crossreactivity of monobodies to the apo-ER alpha-LBD, suggesting a dynamic nature of the ER alpha-LBD conformation and a role of the F domain in restraining the LBD in an inactive conformation.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	3
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Carrier Proteins Chemistry Receptors, Estrogen Amino Acid Sequence Binding Sites Biosynthesis Estrogen Receptor Alpha Estrogens Metabolism Gene Library Genetic Vectors Ligands Mutagenesis, Site-Directed Protein Conformation Recombinant Proteins Saccharomyces Cerevisiae Genetics Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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