Table 3.xls (9.5 kB)
Aromatic interactions and Cation-pi interactions of PKR with the interacting proteins.
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posted on 2016-04-18, 08:53 authored by K. Hari Krishna, Yallamandayya Vadlamudi, Muthuvel Suresh KumarAromatic interactions between the PKR and the interacting proteins formed during the course of simulation within 7 A°. The cation-pi interactions of PKR with the proteins formed during the course of simulation within 6 A°. The minimum distance between the residues is indicated in the brackets.
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K 3LsubstrateKinase Domaininhibitors TATphosphorylation eventsPKR exhibits variationsdynamics studiesbasisactivation loop residuesbinding proteinseIFStructural Perspectivereplication mechanismsRNA Dependent Protein Kinase PKRprotein kinase PKRdomain movementsViral Evolved Inhibition MechanismN lobetranslation initiationinhibitor interaction mechanisms
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