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Protein Sci. 2007 Jul;16(7):1479-84. Epub 2007 Jun 13.

Solution structure of a membrane-anchored ubiquitin-fold (MUB) protein from Homo sapiens.

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1
Department of Biochemistry and Center for Eukaryotic Structural Genomics, Medical College of Wisconsin, Milwaukee 53226, USA.

Abstract

The protein Bc059385, whose solution structure is reported here, is the human representative of a recently identified family of membrane-anchored ubiquitin-fold (MUB) proteins. Analysis of their similarity to ubiquitin indicates that homologous amino acid residues in MUBs form a hydrophobic surface very similar to the recognition patch surrounding Ile-44 in ubiquitin. This suggests that MUBs may interact with proteins containing an alpha-helical motif similar to those of some ubiquitin binding domains. A disordered loop common to MUBs may also provide a second protein interaction site. From the available data, it is probable that this protein is prenylated and associated with the membrane. With <20% identity to ubiquitin, the MUB family further expands the sequence space that maps to the beta-grasp fold, and adds membrane localization to its list of functional roles.

PMID:
17567738
PMCID:
PMC2206703
DOI:
10.1110/ps.072834007
[Indexed for MEDLINE]
Free PMC Article
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