2GOW

Solution structure of BC059385 from Homo sapiens

Summary for 2GOW

• Entry DOI: 10.2210/pdb2gow/pdb
• NMR Information: BMRB: 7095
• Descriptor: Ubiquitin-like protein 3 (1 entity in total)
• Functional Keywords: bc059385, structural genomics, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, unknown function
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Lipid-anchor (By similarity): O95164
• Total number of polymer chains: 1
• Total formula weight: 14169.03

Authors

Volkman, B.F.,de la Cruz, N.B.,Lytle, B.L.,Peterson, F.C.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2006-04-14, release date: 2006-04-25, Last modification date: 2024-05-29)

Primary citation

de la Cruz, N.B.,Peterson, F.C.,Lytle, B.L.,Volkman, B.F.
Solution structure of a membrane-anchored ubiquitin-fold (MUB) protein from Homo sapiens.
Protein Sci., 16:1479-1484, 2007

PubMed 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.

PubMed: 17567738
DOI: 10.1110/ps.072834007

Experimental method

SOLUTION NMR