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


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.

SUBMITTER: de la Cruz NB 

PROVIDER: S-EPMC2206703 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature

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

de la Cruz Norberto B NB   Peterson Francis C FC   Lytle Betsy L BL   Volkman Brian F BF  

Protein science : a publication of the Protein Society 20070613 7


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 d  ...[more]

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