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Table 3 Dimer interface residues in PKR that are mimicked by the residues in HCV NS5A

From: Structural and molecular basis of interaction of HCV non-structural protein 5A with human casein kinase 1α and PKR

Nature of interaction

Dimer interface residues of PKR

Equivalent residues in NS5A

D266 (Ionic interaction)

R262

S249

R262 (Ionic interaction)

D266

D253

C326 (Hydrogen bond : NE2 of His with O of Cys )

H286

T270

Y300, V309 (Hydrophobic interaction)

I288

V272

Y323 (Hydrogen bond: OD2 of Asp with OH of Tyr)

D289

E273

I288, V309 (Hydrophobic interaction)

Y300

F284

  1. The equivalent residues in NS5A to the PKR dimer interface residues are obtained from the pairwise alignment as shown in the Figure6. The equivalent residues in NS5A which are capable of interacting with PKR mimics the binding of PKR protomer to the other PKR protomer due to the shared binding region of NS5A and PKR protomer with another PKR protomer[14].
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BMC Structural Biology

ISSN: 1472-6807

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