Dynactins p25 and p27 are predicted to adopt the LbetaH fold.
Dynactin is a multimeric protein essential for the minus-end-directed transport driven by microtubule-based motor dynein. The pointed-end subcomplex in dynactin contains p62, p27, p25, and Arp11 subunits, and is thought to participate in interactions with membranous cargoes. We used sequence and structure prediction analysis to study dynactins p25 and p27. Here we present evidence that strongly supports that dynactins p27 and p25 contain the isoleucine-patch motif and adopt the left-handed parallel beta-helix fold. The structural models we obtained could contribute to the understanding of the complex interactions that dynactins are able to establish with cargo particles, microtubules or other dynactin subunits.
Parisi
Gustavo
G
Universidad Nacional de Quilmes, Roque Sáenz Peña 180, B1876BXD Bernal, Argentina. gustavo@unq.edu.au
Fornasari
María Silvina
MS
Echave
Julián
J
D000595:Amino Acid Sequence; D000818:Animals; D000072159:Dynactin Complex; D006801:Humans; D008869:Microtubule-Associated Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D021122:Protein Subunits / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment
D000072159:Dynactin Complex; D008869:Microtubule-Associated Proteins; D021122:Protein Subunits