8tt7 | pdb_00008tt7

NMR Assignments and Structure for the Dimeric Kinesin Neck Domain

spinqualitylabelsall models 8tt7 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8tt7 is a 2 chain structure with sequence from Rattus norvegicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KIF5C_RAT Microtubule-associated force-producing protein that may play a role in organelle transport (By similarity). Has ATPase activity (PubMed:27452403). Involved in synaptic transmission (By similarity). Mediates dendritic trafficking of mRNAs (By similarity). Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation (PubMed:23576431).[UniProtKB:O60282][UniProtKB:P28738] Publication Abstract from PubMed Kinesin is a motor protein, comprised of two heavy and two light chains that transports cargo along the cytoskeletal microtubule filament network. The heavy chain has a neck domain connecting the ATPase motor head responsible for walking along microtubules, with the stalk and subsequent tail domains that bind cargo. The neck domain consists of a coiled coli homodimer with about five heptad repeats, preceded by a linker region that joins to the ATPase head. Here we report (1)H, (15)N, and (13)C NMR assignments and a solution structure for the kinesin neck domain from rat isoform Kif5c. The calculation of the NMR structure of the homodimer was facilitated by unambiguously assigning sidechain NOEs between heptad a and d positions to interchain contacts, since these positions are too far apart to give sidechain contacts in the monomers. The dimeric coiled coil NMR structure is similar to the previously described X-ray structure, whereas the linker region is disordered in solution but contains a short segment with beta-strand propensity- the beta-linker. Only the coiled coil is protected from solvent exchange, with ∆G values for hydrogen exchange on the order of 4-6 kcal/mol. The high stability of the hydrogen-bonded alpha-helical structure makes it unlikely that unzippering of the coiled coil is involved in kinesin walking. Rather, the linker region serves as a flexible hinge between the kinesin head and neck. Solution NMR assignments and structure for the dimeric kinesin neck domain.,Seo D, Kammerer RA, Alexandrescu AT Biomol NMR Assign. 2023 Oct 20. doi: 10.1007/s12104-023-10159-x. PMID:37861970 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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