Strategies to control the binding mode of de novo designed protein interactions.

Abstract:

:There has been significant recent progress in the computational design of protein interactions including the creation of novel heterodimers, homodimers, nanohedra, fibril caps and a protein crystal. Essential to these successes has been the use of innovative strategies for finding binding modes that are achievable, that is, identifying binding partners and docked conformations that can be successfully stabilized via sequence optimization and backbone refinement. In many cases this has involved the use of structural motifs commonly found at naturally occurring interfaces including alpha helices inserted into hydrophobic grooves, beta-strand pairing, metal binding, established helix packing motifs, and the use of symmetry to form cooperative interactions. Future challenges include the creation of hydrogen bond networks and antibody-like interactions based on the redesign of protein surface loops.

journal_name

Curr Opin Struct Biol

authors

Der BS,Kuhlman B

doi

10.1016/j.sbi.2013.04.010

subject

Has Abstract

pub_date

2013-08-01 00:00:00

pages

639-46

issue

4

eissn

0959-440X

issn

1879-033X

pii

S0959-440X(13)00078-X

journal_volume

23

pub_type

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