pone.0270572.s006.pdf (3.65 MB)
Download fileStructural variation of PRC1-DD wild-type and mutants mapped to structure, residue R2 is represented in stick representation.
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posted on 05.08.2022, 20:04 authored by Fei Tan, Jin Xu(a) For mutant Δ1R2M, residues with great chemical shift changes compared to wild-type are mapped to PRC1-DD structure. (b) For mutant R2E, areas with great chemical shift changes are mapped to PRC1-DD structure. Red denote areas with chemical shift change of 8 ppm or more, white denotes chemical shift change of around 5 ppm, blue shows no chemical shift change.
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hydrophobic core packingdeuterium exchange experiments>- helix h2proteins called microtubulecycle dependent proteinsn terminal residuesalso generated mutantsdiv >< pconformation prc1 adoptedhigh resolution threeprc1 </ presolution solution structureassociated proteinsn terminusalso differentalpha </prc1 ’prc1 callswhole proteinused hydrogenthermal stabilityspindle midbodysolution structuressolution structureresults suggestplacing hurdlesphysiological significancenmr spectroscopyincomplete sidechainshuman mapfunction relationshipsdistinguishing memberdimerization domaindimensional structurebind microtubules
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