Selected article for: "binding site and crystal structure"

Author: Ma, Wenjun; García-Sastre, Adolfo; Schwemmle, Martin
Title: Expected and Unexpected Features of the Newly Discovered Bat Influenza A-like Viruses
  • Document date: 2015_6_4
  • ID: 11ecey66_3
    Snippet: Biochemical and structural studies indicate that both the influenza A-like H17 and H18 proteins do not bind canonical sialic acid-containing receptors [3] [4] [5] , which are bound by HAs of conventional IAVs for initiation of infection. Furthermore, the crystal structure of H17 and H18 revealed that these proteins possess a distorted putative sialic acid binding site and showed low thermostability when compared to all known well-characterized HA.....
    Document: Biochemical and structural studies indicate that both the influenza A-like H17 and H18 proteins do not bind canonical sialic acid-containing receptors [3] [4] [5] , which are bound by HAs of conventional IAVs for initiation of infection. Furthermore, the crystal structure of H17 and H18 revealed that these proteins possess a distorted putative sialic acid binding site and showed low thermostability when compared to all known well-characterized HAs [3, 5] . In fact, H17 and H18 HAs are unable to bind and hemagglutinate red blood cells and therefore are not "true" HAs. Thus, we suggest that HAs from both H17 and H18 influenza A-like viruses should be named as "HA-like" (HL) proteins (HL17 and HL18).

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