| Literature DB >> 25503290 |
Vaibhav Kumar Shukla1, Ashish Kabra1, Rahul Yadav1, Shoichiro Ono2,3, Dinesh Kumar4, Ashish Arora5.
Abstract
The actin filament dynamics in nematode, Caenorhabditis elegans, is regulated by differential activity of two proteins UNC-60A and UNC-60B. UNC-60A exhibits strong pointed end depolymerization on C. elegans actin (Ce-actin), strong inhibition of polymerization, strong monomer sequestering activity, weak severing activity, and low affinity for F-actin binding, while UNC-60B exhibits strong pointed end depolymerization on rabbit muscle actin, strong severing activity, and high affinity for F-actin binding. Structural characterization of these proteins will help to understand (1) molecular mechanism of actin dynamics regulation and (2) the differential activity of these proteins. Here, we report (1)H, (13)C, and (15)N chemical shift assignments of these two proteins as determined by heteronuclear NMR experiments (at pH 6.5 and temperature 298 K).Entities:
Keywords: ADF like protein; NMR; Resonance assignment; UNC-60A; UNC-60B
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Year: 2014 PMID： 25503290 PMCID： PMC4465417 DOI： 10.1007/s12104-014-9588-5
Source DB: PubMed Journal: Biomol NMR Assign ISSN： 1874-270X Impact factor: 0.746