pone.0270572.s008.docx (5.82 MB)
Download fileTwo-dimensional 1H-15N HSQC spectrum of E49D and E49A compared with wildtype PRC1-DD.
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posted on 05.08.2022, 20:04 authored by Fei Tan, Jin Xu(a) Ribbon representation of solution structure, in which residues E49, H46 and those residues that interact with it were stressed in ball-and-stick representation. (b) crystal structure of PRC1-DD, in which residues E49, H46 and those residues that interact with it were stressed in ball-and-stick representation. (c) The superposition of two-dimensional 1H-15N HSQC spectrum of wildtype(black) and E49D(red), in which residues exhibiting large changes are denoted. (d) The superposition of two-dimensional 1H-15N HSQC spectrum of wildtype(black) and E49A(red), in which residues exhibiting large changes are denoted.
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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