K Van Roey, B Uyar, RJ Weatheritt, H Dinkel… - Chemical …, 2014 - ACS Publications
The eukaryotic cell is a bustling collection of macromolecules acting cooperatively to mediate the functions required for cell viability. Specific, context-dependent and tightly …
N Kurochkina, U Guha - Biophysical reviews, 2013 - Springer
Abstract Src homology 3 (SH3) domains are involved in the regulation of important cellular pathways, such as cell proliferation, migration and cytoskeletal modifications. Recognition of …
The PDZ domain is a protein–protein interacting module that plays an important role in the organization of signaling complexes. The recognition of short intrinsically disordered C …
C Yang, S Zhang, P He, C Wang… - Journal of Chemical …, 2015 - ACS Publications
Self-binding peptides (SBPs) represent those short peptide segments within monomeric proteins to fulfill their biological functions by dynamically binding to/unbinding from their …
K Luck, S Charbonnier, G Travé - FEBS letters, 2012 - Elsevier
The canonical binding mode of PDZ domains to target motifs involves a small interface, unlikely to fully account for PDZ-target interaction specificities. Here, we review recent work …
C Yang, S Zhang, Z Bai, S Hou, D Wu, J Huang… - Molecular …, 2016 - pubs.rsc.org
Self-binding peptides (SBPs) represent a novel biomolecular phenomenon spanning between folding and binding, where a short peptide segment within a monomeric protein …
T Hagai, A Azia, MM Babu, R Andino - Cell reports, 2014 - cell.com
Viruses interact extensively with host proteins, but the mechanisms controlling these interactions are not well understood. We present a comprehensive analysis of eukaryotic …
Short linear motifs (SLiMs) are protein interaction sites that play an important role in cell regulation by controlling protein activity, localization, and local abundance. The functionality …
Highlights•Accrual of peptide–protein complex structures allowed their detailed characterization.•This has lead to rapid progress in peptide docking, based on diverse …