2v71

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
|PDB= 2v71 |SIZE=350|CAPTION= <scene name='initialview01'>2v71</scene>, resolution 2.24&Aring;
|PDB= 2v71 |SIZE=350|CAPTION= <scene name='initialview01'>2v71</scene>, resolution 2.24&Aring;
|SITE=
|SITE=
-
|LIGAND=
+
|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v71 OCA], [http://www.ebi.ac.uk/pdbsum/2v71 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v71 RCSB]</span>
}}
}}
Line 40: Line 43:
[[Category: transport]]
[[Category: transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:43:40 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:09:00 2008''

Revision as of 02:09, 31 March 2008

Image:2v71.gif


PDB ID 2v71

Drag the structure with the mouse to rotate
, resolution 2.24Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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 Mon Mar 31 05:09:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v71"
Personal tools