Publication Abstract from PubMed
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.
Solution structure of a membrane-anchored ubiquitin-fold (MUB) protein from Homo sapiens.,de la Cruz NB, Peterson FC, Lytle BL, Volkman BF Protein Sci. 2007 Jul;16(7):1479-84. Epub 2007 Jun 13. PMID:17567738[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
