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Published online before print June 13, 2007, 10.1110/ps.072834007
Protein Science (2007), 16:1479-1484. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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PROTEIN STRUCTURE REPORT

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

Norberto B. de la Cruz, Francis C. Peterson, Betsy L. Lytle, and Brian F. Volkman

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

(RECEIVED February 19, 2007; FINAL REVISION March 28, 2007; ACCEPTED April 2, 2007)

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.

Keywords: structural genomics; NMR; beta-grasp; CAAX box; prenylation; ubiquitin binding domain


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