Molecular analysis of muskelin identifies a conserved discoidin-like domain that contributes to protein self-association
| Autor: | Soren Prag, Josephine C. Adams, Georgina D. M. Collett |
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| Rok vydání: | 2004 |
| Předmět: |
Repetitive Sequences
Amino Acid Architecture domain Myoblasts Skeletal Molecular Sequence Data Protozoan Proteins Sequence alignment Biology Kidney Transfection Biochemistry Conserved sequence Cell Line Avian Proteins Mice Phylogenetics Lectins Extracellular Animals Drosophila Proteins Humans Amino Acid Sequence Molecular Biology Peptide sequence Cellular localization Conserved Sequence Zebrafish Genetics Intracellular Signaling Peptides and Proteins Proteins Cell Biology Zebrafish Proteins Cell biology Ciona intestinalis Protein Structure Tertiary Rats Peptides Cell Adhesion Molecules Dimerization Discoidins Sequence Alignment Drosophila Protein Research Article |
| Zdroj: | The Biochemical journal. 381(Pt 2) |
| ISSN: | 1470-8728 |
| Popis: | 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 have been shown to self-associate, co-immunoprecipitation, protein pull-down assays and studies of cellular localization were carried out with wild-type, deletion mutant and point mutant muskelins to investigate the roles of the discoidin-like and kelch-repeat domains. We obtained evidence for cis- and trans-interactions between the two domains. These studies provide evidence that muskelin self-associates through a head-to-tail mechanism involving the discoidin-like domain. |
| Databáze: | OpenAIRE |
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