Solution structure of a membrane-anchored ubiquitin-fold (MUB) protein from Homo sapiens. Protein Sci 2007 Jul;16(7):1479-84
Date
06/15/2007Pubmed ID
17567738Pubmed Central ID
PMC2206703DOI
10.1110/ps.072834007Scopus ID
2-s2.0-34250837588 (requires institutional sign-in at Scopus site) 6 CitationsAbstract
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.
Author List
de la Cruz NB, Peterson FC, Lytle BL, Volkman BFAuthors
Francis C. Peterson PhD Professor in the Biochemistry department at Medical College of WisconsinBrian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
Cell MembraneHumans
Hydrophobic and Hydrophilic Interactions
Magnetic Resonance Spectroscopy
Membrane Proteins
Models, Molecular
Protein Binding
Protein Folding
Protein Prenylation
Solutions
Ubiquitin
