ArticleActa crystallographica. Section F, Structural biology communications2014
Crystallographic characterization of the C-terminal coiled-coil region of mouse Bicaudal-D1 (BICD1).
Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- BICD1 mediates HIF1α nuclear translocation in mesenchymal stem cells during hypoxia adaptation.Cell death and differentiation · 2019Article
- Exploring the Molecular Mechanism of Thoracic Aortic Aneurysm via Bioinformatics Analysis.Medical science monitor : international medical journal of experimental and clinical research · 2018Article
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Abstract
Bicaudal-D1 (BICD1) is an α-helical coiled-coil protein which is evolutionarily conserved from Drosophila to mammals and facilitates the attachment of specific cargo factors to the dynein motor complex. The C-terminal coiled-coil region (CC3) of BICD1 plays an important role in sorting cargo, linking proteins such as the small GTPase Rab6 and the nuclear pore complex component Ran-binding protein 2 (RanBP2) to the dynein motor complex. This report describes the crystallization and X-ray data collection of the BICD1 CC3 region, as well as the preparation of the complex of BICD1 CC3 with a constitutively active mutant of Rab6. The crystals of the BICD1 CC3 region belonged to space group C2, with unit-cell parameters a = 59.0, b = 36.8, c = 104.3 Å, α = γ = 90, β = 99.8°. The X-ray diffraction data set was collected to 1.50 Å resolution.
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