Peptide docking and structure-based characterization of peptide binding: from knowledge to know-how.

Abstract:

:Peptide-mediated interactions are gaining increased attention due to their predominant roles in the many regulatory processes that involve dynamic interactions between proteins. The structures of such interactions provide an excellent starting point for their characterization and manipulation, and can provide leads for targeted inhibitor design. The relatively few experimentally determined structures of peptide-protein complexes can be complemented with an outburst of modeling approaches that have been introduced in recent years, with increasing accuracy and applicability to ever more systems. We review different methods to address the considerable challenges in modeling the binding of a short yet highly flexible peptide to its partner. These methods apply an array of sampling strategies and draw from a recent amassing of knowledge about the biophysical nature of peptide-protein interactions. We elaborate on applications of these structure-based approaches and in particular on the characterization of peptide binding specificity to different peptide-binding domains and enzymes. Such applications can identify new biological targets and thus complement our current view of protein-protein interactions in living organisms. Accurate peptide-protein docking is of particular importance in the light of increased appreciation of the crucial functional roles of disordered regions and the many linear binding motifs embedded within.

journal_name

Curr Opin Struct Biol

authors

London N,Raveh B,Schueler-Furman O

doi

10.1016/j.sbi.2013.07.006

subject

Has Abstract

pub_date

2013-12-01 00:00:00

pages

894-902

issue

6

eissn

0959-440X

issn

1879-033X

pii

S0959-440X(13)00127-9

journal_volume

23

pub_type

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