2ncd

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

spinqualitylabelsall models 2ncd, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ncd is a 1 chain structure with sequence from Drosophila melanogaster. The April 2005 RCSB PDB Molecule of the Month feature on Kinesin by David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, SO4 Gene: NCD (Drosophila melanogaster) Resources: FirstGlance, OCA, RCSB, PDBsum Function [NCD_DROME] NCD is required for normal chromosomal segregation in meiosis, in females, and in early mitotic divisions of the embryo. The NCD motor activity is directed toward the microtubule's minus end. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Kinesin

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