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Human β-cardiac myosin exists in an ON-state where both myosin heads are accessible for interaction with actin, and an OFF-state where the heads are folded back onto ...
2012). Mutation and deletion of the PTPIP51 coiled-coil domain but not the FFAT motif markedly affects the binding of PTPIP51 to VAPB in cellular immunoprecipitation assays To probe the roles of the ...
This flexibility and the relatively poor adherence to the heptad repeat pattern may explain why this domain can be disrupted by a single point mutation, whereas often coiled-coil interactions are more ...
Created with BioRender.com. (C) Sanger sequencing from samples at the indicated timepoints confirms the acquisition of an A to C mutation in CARD11, which results in the activating, coiled-coil domain ...
The autoinhibited conformation of kinesin-3 is predominantly mediated by a coiled-coil ... Mutations of the essential residues in the interdomain interaction interface in the MD-NC-CC1 monomer ...
L1ORF1p contains an essential, but rapidly evolving N-terminal portion, homo-trimerizes via a coiled coil and packages L1RNA into large assemblies. Here, we determined crystal structures of the entire ...
ClpC forms large two-helical assemblies that associate via head-to-head contacts between coiled-coil middle domains (MDs ... also studied ClpC proteins that had mutations to the middle domain that ...
Mutations in the MURC/Cavin-4 gene have been identified in patients with dilated cardiomyopathy. MURC/Cavin-4 has the coiled-coil domain; however, its functional significance remains unknown. [Methods ...
In this study, we constructed rad50 alleles encoding truncations of the coiled-coil domain to determine which Mre11 complex functions required the full length of the coils. These mutations ...
Here, we report the discovery of two secondary mutations within the kinase domain ... dimerization through interaction between the coiled-coil domain within the EML4 region of each monomer ...
The scientists found that all of the mutations caused changes in amino acids in a small segment of the CARD11 protein known as the coiled-coil domain, which is required for proper CARD11 function.
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