2v66
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(New page: 200px<br /><applet load="2v66" size="350" color="white" frame="true" align="right" spinBox="true" caption="2v66, resolution 2.10Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 10:00, 23 January 2008
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CRYSTAL STRUCTURE OF THE COILED-COIL DOMAIN OF NDEL1 (A.A. 58 TO 169)C
Overview
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.
About this Structure
2V66 is a Single protein structure of sequence from Homo sapiens with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
The structure of the coiled-coil domain of ndel1 and the basis of its interaction with lis1, the causal protein of miller-dieker lissencephaly., Derewenda U, Tarricone C, Choi WC, Cooper DR, Lukasik S, Perrina F, Tripathy A, Kim MH, Cafiso DS, Musacchio A, Derewenda ZS, Structure. 2007 Nov;15(11):1467-81. PMID:17997972
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