2ncd

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spinqualitylabelsall models PDB ID 2ncd Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
2ncd, resolution 2.50Å ()
Ligands:	,
Gene:	NCD (Drosophila melanogaster)
Structural annotation: Resources: CATH : 2Ncda00 InterPro : Ipr001752 Pfam : PF00225 SCOP : d2ncda_ UniProt : P20480
Functional annotation: Cellular component: microtubule microtubule associated complex spindle Biological process: mitotic spindle elongation spindle assembly involved in female meiosis cell division microtubule-based movement mitosis cell cycle mitotic centrosome separation meiotic spindle organization and biogenesis distributive segregation meiosis Molecular function: minus-end-directed microtubule motor activity motor activity microtubule motor activity protein binding nucleotide binding ATP binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

NCD (NON-CLARET DISJUNCTIONAL) DIMER FROM D. MELANOGASTER

Overview

Motor proteins of the kinesin superfamily transport intracellular cargo along microtubules. Although different kinesin proteins share 30-50% amino-acid identity in their motor catalytic cores, some move to the plus end of microtubules whereas others travel in the opposite direction. Crystal structures of the catalytic cores of conventional kinesin (a plus-end-directed motor involved in organelle transport) and ncd (a minus-end-directed motor involved in chromosome segregation) are nearly identical; therefore, the structural basis for their opposite directions of movement is unknown. Here we show that the ncd 'neck' made up of 13 class-specific residues next to the superfamily-conserved catalytic core, is essential for minus-end-directed motility, as mutagenesis of these neck residues reverses the direction of ncd motion. By solving the 2.5 A structure of a functional ncd dimer, we show that the ncd neck (a coiled-coil) differs from the corresponding region in the kinesin neck (an interrupted beta-strand), although both necks interact with similar elements in the catalytic cores. The distinct neck architectures also confer different symmetries to the ncd and kinesin dimers and position these motors with appropriate directional bias on the microtubule.

About this Structure

2NCD is a Single protein structure of sequence from Drosophila melanogaster. The following page contains interesting information on the relation of 2NCD with [Kinesin]. Full crystallographic information is available from OCA.

Reference

Direction determination in the minus-end-directed kinesin motor ncd., Sablin EP, Case RB, Dai SC, Hart CL, Ruby A, Vale RD, Fletterick RJ, Nature. 1998 Oct 22;395(6704):813-6. PMID:9796817 Page seeded by OCA on Sun May 4 09:35:32 2008