4YTD

Crystal structure of the C-terminal Coiled Coil of mouse Bicaudal D1

Summary for 4YTD

• Entry DOI: 10.2210/pdb4ytd/pdb
• Descriptor: Protein bicaudal D homolog 1, PHOSPHATE ION (3 entities in total)
• Functional Keywords: retrograde transport, cytoplasmic dynein, bicaudal d1, coiled coil, cargo binding, transport protein
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 2
• Total formula weight: 24309.46

Authors

Terawaki, S.,Yoshikane, A.,Higuchi, Y.,Wakamatsu, K. (deposition date: 2015-03-17, release date: 2015-04-08, Last modification date: 2020-02-05)

Primary citation

Terawaki, S.I.,Yoshikane, A.,Higuchi, Y.,Wakamatsu, K.
Structural basis for cargo binding and autoinhibition of Bicaudal-D1 by a parallel coiled-coil with homotypic registry
Biochem.Biophys.Res.Commun., 460:451-456, 2015

PubMed Abstract: Bicaudal-D1 (BICD1) is an α-helical coiled-coil protein mediating the attachment of specific cargo to cytoplasmic dynein. It plays an essential role in minus end-directed intracellular transport along microtubules. The third C-terminal coiled-coil region of BICD1 (BICD1 CC3) has an important role in cargo sorting, including intracellular vesicles associating with the small GTPase Rab6 and the nuclear pore complex Ran binding protein 2 (RanBP2), and inhibiting the association with cytoplasmic dynein by binding to the first N-terminal coiled-coil region (CC1). The crystal structure of BICD1 CC3 revealed a parallel homodimeric coiled-coil with asymmetry and complementary knobs-into-holes interactions, differing from Drosophila BicD CC3. Furthermore, our binding study indicated that BICD1 CC3 possesses a binding surface for two distinct cargos, Rab6 and RanBP2, and that the CC1-binding site overlaps with the Rab6-binding site. These findings suggest a molecular basis for cargo recognition and autoinhibition of BICD proteins during dynein-dependent intracellular retrograde transport.

PubMed: 25796327
DOI: 10.1016/j.bbrc.2015.03.054

Experimental method

X-RAY DIFFRACTION (1.5 Å)