54 0

Structure of a nanobody-stabilized active state of the beta(2) adrenoceptor

Title
Structure of a nanobody-stabilized active state of the beta(2) adrenoceptor
Author
채필석
Keywords
PROTEIN-COUPLED RECEPTOR; CRYSTAL-STRUCTURE; BETA(2)-ADRENERGIC RECEPTOR; ADRENERGIC-RECEPTOR; LIGAND-BINDING; ACTIVATION; RHODOPSIN; OPSIN; CONFORMATIONS
Issue Date
2011-01
Publisher
Nature Publishing Group
Citation
Nature, 2011, 469, P.175-180
Abstract
G protein coupled receptors (GPCRs) exhibit a spectrum of functional behaviours in response to natural and synthetic ligands. Recent crystal structures provide insights into inactive states of several GPCRs. Efforts to obtain an agonist-bound active-state GPCR structure have proven difficult due to the inherent instability of this state in the absence of a G protein. We generated a camelid antibody fragment (nanobody) to the human beta(2) adrenergic receptor (beta(2)AR) that exhibits G protein-like behaviour, and obtained an agonist-bound, active-state crystal structure of the receptor-nanobody complex. Comparison with the inactive beta(2)AR structure reveals subtle changes in the binding pocket; however, these small changes are associated with an 11 angstrom outward movement of the cytoplasmic end of transmembrane segment 6, and rearrangements of transmembrane segments 5 and 7 that are remarkably similar to those observed in opsin, an active form of rhodopsin. This structure provides insights into the process of agonist binding and activation.
URI
https://www.nature.com/articles/nature09648
ISSN
0028-0836; 1476-4687
DOI
10.1038/nature09648
Appears in Collections:
GRADUATE SCHOOL[S](대학원) > BIONANOTECHNOLOGY(바이오나노학과) > Articles
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE