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Guanidinobenzoic acid inhibitors of influenza virus neuraminidase.

Abstract：

:The active site of influenza virus neuraminidase (NA) is formed by 11 universally conserved residues. A guanidino group incorporated into two unrelated NA inhibitors was previously reported to occupy different negatively charged sites in the NA active site, A new inhibitor containing two guanidino groups was synthesized in order to utilize both sites in an attempt to acquire a combined increase in affinity. The X-ray crystal structures of the complexes show that the expected increase in affinity could not be achieved even though the added guanidino group binds to the negatively charged site as designed. This suggests that the ligand affinity to the target protein is contributed both from ligand-protein interactions and solvation/conformation energy of the ligand.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Sudbeck EA,Jedrzejas MJ,Singh S,Brouillette WJ,Air GM,Laver WG,Babu YS,Bantia S,Chand P,Chu N,Montgomery JA,Walsh DA,Luo M

doi

10.1006/jmbi.1996.0885

subject

Has Abstract

pub_date

1997-04-04 00:00:00

pages

584-94

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(96)90885-2

journal_volume

267

pub_type

杂志文章

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