de la Cruz Norberto B, Peterson Francis C, Lytle Betsy L, Volkman Brian F
Department of Biochemistry and Center for Eukaryotic Structural Genomics, Medical College of Wisconsin, Milwaukee 53226, USA.
Protein Sci. 2007 Jul;16(7):1479-84. doi: 10.1110/ps.072834007. Epub 2007 Jun 13.
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.
本文报道了其溶液结构的蛋白质Bc059385，是最近鉴定出的膜锚定泛素折叠（MUB）蛋白家族的人类代表。对其与泛素相似性的分析表明，MUB中的同源氨基酸残基形成了一个疏水表面，与泛素中围绕Ile-44的识别区域非常相似。这表明MUB可能与含有类似于某些泛素结合结构域的α-螺旋基序的蛋白质相互作用。MUB共有的无序环也可能提供第二个蛋白质相互作用位点。根据现有数据，这种蛋白质可能被异戊二烯化并与膜相关。MUB家族与泛素的同源性小于20%，进一步扩展了映射到β-抓握折叠的序列空间，并将膜定位添加到其功能作用列表中。
