| First Author | Collins MN | Year | 2011 |
| Journal | Structure | Volume | 19 |
| Issue | 3 | Pages | 324-36 |
| PubMed ID | 21397184 | Mgi Jnum | J:245302 |
| Mgi Id | MGI:5916903 | Doi | 10.1016/j.str.2010.11.017 |
| Citation | Collins MN, et al. (2011) Structural characterization of the Boca/Mesd maturation factors for LDL-receptor-type beta propeller domains. Structure 19(3):324-36 |
| abstractText | Folding and trafficking of low-density lipoprotein receptor (LDLR) family members, which play essential roles in development and homeostasis, are mediated by specific chaperones. The Boca/Mesd chaperone family specifically promotes folding and trafficking of the YWTD beta propeller-EGF domain pair found in the ectodomain of all LDLR members. Limited proteolysis, NMR spectroscopy, analytical ultracentrifugation, and X-ray crystallography were used to define a conserved core composed of a structured domain that is preceded by a disordered N-terminal region. High-resolution structures of the ordered domain were determined for homologous proteins from three metazoans. Seven independent protomers reveal a novel ferrodoxin-like superfamily fold with two distinct beta sheet topologies. A conserved hydrophobic surface forms a dimer interface in each crystal, but these differ substantially at the atomic level, indicative of nonspecific hydrophobic interactions that may play a role in the chaperone activity of the Boca/Mesd family. |
