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 ¹H, ^(15)N, and ^(13)C...
[NMR paper] NMR assignment and dynamics of the dimeric form of soluble C-terminal domain major ampullate spidroin 2 from Latrodectus hesperus
NMR assignment and dynamics of the dimeric form of soluble C-terminal domain major ampullate spidroin 2 from Latrodectus hesperus
Spider dragline silk has attracted great interest due to its outstanding mechanical properties, which exceed those of man-made synthetic materials. Dragline silk, which is composed of at least major ampullate spider silk protein 1 and 2 (MaSp1 and MaSp2), contains a long repetitive domain flanked by N-terminal and C-terminal domains (NTD and CTD). Despite the small size of the CTD, this domain plays a crucial role as a molecular switch that regulates and directs...
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09-06-2023 01:37 AM
[NMR paper] 1H, 15N and 13C backbone and side chain solution NMR assignments of the TPM domain-containing protein of the thermophilic bacterium Rhodothermus marinus
1H, 15N and 13C backbone and side chain solution NMR assignments of the TPM domain-containing protein of the thermophilic bacterium Rhodothermus marinus
The InterPro family IPR007621 TPM_phosphatase is a widely conserved family of protein domains found in prokaryotes, plants and invertebrates. Despite similar predicted protein folding, members of this family are involved in different cellular processes. In recent years, the structural and biochemical characterization of evolutionarily divergent TPM domains has shown their ability to hydrolyze phosphate groups of different substrates....
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08-06-2023 03:39 PM
[NMR paper] Magic-angle-spinning NMR structure of the kinesin-1 motor domain assembled with microtubules reveals the elusive neck linker orientation
Magic-angle-spinning NMR structure of the kinesin-1 motor domain assembled with microtubules reveals the elusive neck linker orientation
Microtubules (MTs) and their associated proteins play essential roles in maintaining cell structure, organelle transport, cell motility, and cell division. Two motors, kinesin and cytoplasmic dynein link the MT network to transported cargos using ATP for force generation. Here, we report an all-atom NMR structure of nucleotide-free kinesin-1 motor domain (apo-KIF5B) in complex with paclitaxel-stabilized microtubules using magic-angle-spinning (MAS) NMR...
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11-11-2022 06:10 AM
[NMR paper] Solution NMR backbone assignments of disordered Olduvai protein domain CON1 employing Halpha-detected experiments
Solution NMR backbone assignments of disordered Olduvai protein domain CON1 employing Halpha-detected experiments
Olduvai protein domains, encoded by the NBPF gene family, are responsible for the largest increase in copy number of any protein-coding region in the human genome. This has spawned various genetics studies which have linked these domains to human brain development and divergence from our primate ancestors, as well as currently relevant cognitive diseases such as schizophrenia and autism spectrum disorder (ASD). There are six separate Olduvai domains which together form the...
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02-01-2022 04:45 PM
[NMR paper] Dimeric switch of Hakai-truncated monomers during substrate recognition: insights from solution studies and NMR structure.
Dimeric switch of Hakai-truncated monomers during substrate recognition: insights from solution studies and NMR structure.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_final.gif Related Articles Dimeric switch of Hakai-truncated monomers during substrate recognition: insights from solution studies and NMR structure.
J Biol Chem. 2014 Sep 12;289(37):25611-23
Authors: Mukherjee M, Jing-Song F, Ramachandran S, Guy GR, Sivaraman J
Abstract
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[NMR paper] Sequential 1H NMR assignments and secondary structure of an IgG-binding domain from p
Sequential 1H NMR assignments and secondary structure of an IgG-binding domain from protein G.
Related Articles Sequential 1H NMR assignments and secondary structure of an IgG-binding domain from protein G.
Biochemistry. 1991 Jun 4;30(22):5335-40
Authors: Lian LY, Yang JC, Derrick JP, Sutcliffe MJ, Roberts GC, Murphy JP, Goward CR, Atkinson T
Protein G is a member of a class of cell surface bacterial proteins from Streptococcus that bind IgG with high affinity. A fragment of molecular mass 6988, which retains IgG-binding activity, has been...
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08-21-2010 11:16 PM
[NMR paper] Sequential 1H NMR assignments and secondary structure of the B domain of staphylococc
Sequential 1H NMR assignments and secondary structure of the B domain of staphylococcal protein A: structural changes between the free B domain in solution and the Fc-bound B domain in crystal.
Related Articles Sequential 1H NMR assignments and secondary structure of the B domain of staphylococcal protein A: structural changes between the free B domain in solution and the Fc-bound B domain in crystal.
Biochemistry. 1990 Sep 18;29(37):8787-93
Authors: Torigoe H, Shimada I, Saito A, Sato M, Arata Y
The recombinant B domain (FB) of staphylococcal...
Solution NMR assignments and structure for the dimeric kinesin neck domain
Linear Mode
