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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.