Premium
Inside Back Cover: An Unusual Protein–Protein Interaction through Coupled Unfolding and Binding (Angew. Chem. Int. Ed. 37/2014)
Author(s) -
Yu TaeKyung,
Shin SeungA,
Kim EunHee,
Kim Sunghyun,
Ryu KyungSeok,
Cheong Haekap,
Ahn HeeChul,
Jon Sangyong,
Suh JeongYong
Publication year - 2014
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201406161
Subject(s) - folding (dsp implementation) , cover (algebra) , chemistry , protein folding , biophysics , plasma protein binding , binding site , crystallography , peptide , biochemistry , biology , engineering , mechanical engineering , electrical engineering
Protein–protein interactions can involve the folding of a disordered region to form the binding interface. In their Communication on page 9784 ff. , J. Y. Suh and co‐workers report the opposite case, in which binding is accompanied by local unfolding. The structure of an engineered peptide bound to fibronectin extradomain B reveals coupled unfolding and binding through β‐strand displacement. The unfolding exposes a hydrophobic surface that provides key interactions for the complex.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom