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8TT7

NMR Assignments and Structure for the Dimeric Kinesin Neck Domain

Summary for 8TT7
Entry DOI10.2210/pdb8tt7/pdb
NMR InformationBMRB: 52075
DescriptorKinesin heavy chain isoform 5C (1 entity in total)
Functional Keywordsmicrotubule motors, intracellular transport, motor protein
Biological sourceRattus norvegicus (Norway rat)
Total number of polymer chains2
Total formula weight12676.49
Authors
Alexandrescu, A.T. (deposition date: 2023-08-12, release date: 2023-11-01, Last modification date: 2024-05-15)
Primary citationSeo, D.,Kammerer, R.A.,Alexandrescu, A.T.
Solution NMR assignments and structure for the dimeric kinesin neck domain.
Biomol.Nmr Assign., 17:301-307, 2023
Cited by
PubMed Abstract: 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 H, N, and 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 β-strand propensity- the β-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 α-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.
PubMed: 37861970
DOI: 10.1007/s12104-023-10159-x
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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