The SCHOOL of nature: II. Protein order, disorder and oligomericity in transmembrane signaling.

ABSTRACT: Recent reports have revealed that many proteins that do not adopt globular structures under native conditions, thus termed intrinsically disordered proteins (IDPs), are involved in cell signaling. Intriguingly, physiologically relevant oligomerization of IDPs has been recently observed and shown to exhibit unique biophysical characteristics, including the lack of significant changes in chemical shift and peak intensity upon binding. In this work, I summarize several distinct features of protein disorder that are especially important as related to receptor-mediated transmembrane signal transduction. I also hypothesize that interactions of IDPs with their protein or lipid partners represent a general biphasic process with the "no disorder-to-order" fast interaction which, depending on the in

SUBMITTER: Sigalov AB 

PROVIDER: S-EPMC3065667 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature