2V66

Crystal Structure of the coiled-coil domain of Ndel1 (a.a. 58 to 169) C

Summary for 2V66

• Entry DOI: 10.2210/pdb2v66/pdb
• Descriptor: NUCLEAR DISTRIBUTION PROTEIN NUDE-LIKE 1, MERCURY (II) ION (3 entities in total)
• Functional Keywords: structural protein, developmental protein, structural protein phosphorylation, transport, microtubule, neurogenesis, cytoskeleton, differentiation
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm, cytoskeleton: Q9GZM8
• Total number of polymer chains: 4
• Total formula weight: 53067.22

Authors

Tarricone, C.,Perrina, F.,Musacchio, A. (deposition date: 2007-07-13, release date: 2007-11-27, Last modification date: 2024-05-08)

Primary citation

Derewenda, U.,Tarricone, C.,Choi, W.C.,Cooper, D.R.,Lukasik, S.,Perrina, F.,Tripathy, A.,Kim, M.H.,Cafiso, D.S.,Musacchio, A.,Derewenda, Z.S.
The Structure of the Coiled-Coil Domain of Ndel1 and the Basis of its Interaction with Lis1, the Causal Protein of Miller-Dieker Lissencephaly.
Structure, 15:1467-, 2007

PubMed Abstract: Ndel1 and Nde1 are homologous and evolutionarily conserved proteins, with critical roles in cell division, neuronal migration, and other physiological phenomena. These functions are dependent on their interactions with the retrograde microtubule motor dynein and with its regulator Lis1--a product of the causal gene for isolated lissencephaly sequence (ILS) and Miller-Dieker lissencephaly. The molecular basis of the interactions of Ndel1 and Nde1 with Lis1 is not known. Here, we present a crystallographic study of two fragments of the coiled-coil domain of Ndel1, one of which reveals contiguous high-quality electron density for residues 10-166, the longest such structure reported by X-ray diffraction at high resolution. Together with complementary solution studies, our structures reveal how the Ndel1 coiled coil forms a stable parallel homodimer and suggest mechanisms by which the Lis1-interacting domain can be regulated to maintain a conformation in which two supercoiled alpha helices cooperatively bind to a Lis1 homodimer.

PubMed: 17997972
DOI: 10.1016/J.STR.2007.09.015

Experimental method

X-RAY DIFFRACTION (2.1 Å)