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 folding mechanism is unaltered, but the folding nucleus has moved within the hydrophobic core.

journal_name

J Mol Biol

authors

Lappalainen I,Hurley MG,Clarke J

doi

10.1016/j.jmb.2007.09.088

subject

Has Abstract

pub_date

2008-01-11 00:00:00

pages

547-59

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(07)01300-9

journal_volume

375

pub_type

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