2v71
From Proteopedia
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| - | [[Image:2v71.gif|left|200px]] | + | [[Image:2v71.gif|left|200px]] |
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| - | '''COILED-COIL REGION OF NUDEL''' | + | {{Structure |
| + | |PDB= 2v71 |SIZE=350|CAPTION= <scene name='initialview01'>2v71</scene>, resolution 2.24Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''COILED-COIL REGION OF NUDEL''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2V71 is a [ | + | 2V71 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V71 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17997972 17997972] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:43:40 2008'' |
Revision as of 16:43, 20 March 2008
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COILED-COIL REGION OF NUDEL
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
2V71 is a Single protein structure of sequence from Rattus norvegicus. 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
Page seeded by OCA on Thu Mar 20 18:43:40 2008
Categories: Rattus norvegicus | Single protein | Cooper, D R. | Derewenda, U. | Derewenda, Z S. | Kim, M H. | Alternative splicing | Coiled coil | Cytoplasm | Cytoskeleton | Developmental protein | Differentiation | Lis1 binding | Microtubule | Microtubule associated migration | Neurogenesis | Nuclear protein | Phosphorylation | Transport
