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Solution structure of a membrane‐anchored ubiquitin‐fold (MUB) protein from Homo sapiens
Author(s) -
de la Cruz Norberto B.,
Peterson Francis C.,
Lytle Betsy L.,
Volkman Brian F.
Publication year - 2007
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.072834007
Subject(s) - ubiquitin , membrane protein , peptide sequence , biology , homo sapiens , protein structure , biochemistry , threading (protein sequence) , chemistry , microbiology and biotechnology , membrane , computational biology , gene , sociology , anthropology
The protein Bc059385, whose solution structure is reported here, is the human representative of a recently identified family of m embrane‐anchored ub iquitin‐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 α‐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 β‐grasp fold, and adds membrane localization to its list of functional roles.