Plasticity within the obligatory folding nucleus of an immunoglobulin-like domain.

ABSTRACT: A number of beta-sandwich immunoglobulin-like domains have been shown to fold using a set of structurally equivalent residues that form a folding nucleus deep within the core of the protein. Formation of this nucleus is sufficient to establish the complex Greek key topology of the native state. These nucleating residues are highly conserved within the immunoglobulin superfamily, but are less well conserved in the fibronectin type III (fnIII) superfamily, where the requirement is simply to have four interacting hydrophobic residues. However, there are rare examples where this nucleation pattern is absent. In this study, we have investigated the folding of a novel member of the fnIII superfamily whose nucleus appears to lack one of the four buried hydrophobic residues. We show that the foldi

SUBMITTER: Lappalainen I 

PROVIDER: S-EPMC2291451 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature