Author: Paesen, Guido C.; Collet, Axelle; Sallamand, Corinne; Debart, Françoise; Vasseur, Jean-Jacques; Canard, Bruno; Decroly, Etienne; Grimes, Jonathan M.
Title: X-ray structure and activities of an essential Mononegavirales L-protein domain Document date: 2015_11_9
ID: 1taxqkk2_18
Snippet: In conclusion, CR-VI þ is a dynamic part of the L protein that potentially completes PRNTase-initiated cap addition, and methylates the cap at its 2 0 O and N7 positions. The SUB P pocket, which is conserved among Paramyxoviridae and Filoviridae (Fig. 6b) , is clearly instrumental in key activities of the domain, and thus represents an attractive target for the structure-based design of (potentially broad-spectrum) antiviral compounds......
Document: In conclusion, CR-VI þ is a dynamic part of the L protein that potentially completes PRNTase-initiated cap addition, and methylates the cap at its 2 0 O and N7 positions. The SUB P pocket, which is conserved among Paramyxoviridae and Filoviridae (Fig. 6b) , is clearly instrumental in key activities of the domain, and thus represents an attractive target for the structure-based design of (potentially broad-spectrum) antiviral compounds.
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