Molecular analysis of muskelin identifies a conserved discoidin-like domain that contributes to protein self-association.

ABSTRACT: Muskelin is an intracellular protein with a C-terminal kelch-repeat domain that was initially characterized as having functional involvement in cell spreading on the extracellular matrix glycoprotein thrombospondin-1. As one approach to understanding the functional properties of muskelin, we have combined bioinformatic and biochemical studies. Through analysis of a new dataset of eight animal muskelins, we showed that the N-terminal region of the polypeptide corresponds to a predicted discoidin-like domain. This domain architecture is conserved in fungal muskelins and reveals a structural parallel between the muskelins and certain extracellular fungal galactose oxidases, although the phylogeny of the two groups appears distinct. In view of the fact that a number of kelch-repeat proteins ha

SUBMITTER: Prag S 

PROVIDER: S-EPMC1133863 | biostudies-literature | 2004 Jul

REPOSITORIES: biostudies-literature