5W5U
Crystal structure of the A/Puerto Rico/8/1934 (H1N1) influenza virus hemagglutinin in complex with cyclic peptide CP141037 (P4)
Summary for 5W5U
| Entry DOI | 10.2210/pdb5w5u/pdb |
| Related | 5w5s 5w6i 5w6r 5w6t 5w6u |
| Descriptor | Hemagglutinin, ACE-PH8-ORN-MLE-GLU-TYR-PHE-GLU-TRP-LEU-SER-BAL, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | glycoprotein, ectodomain, n-glycosylation, viral protein |
| Biological source | Influenza A virus (A/Puerto Rico/8/1934(H1N1)) More |
| Total number of polymer chains | 3 |
| Total formula weight | 59655.53 |
| Authors | Wilson, I.A.,Kadam, R.U. (deposition date: 2017-06-15, release date: 2017-10-04, Last modification date: 2023-11-15) |
| Primary citation | Kadam, R.U.,Juraszek, J.,Brandenburg, B.,Buyck, C.,Schepens, W.B.G.,Kesteleyn, B.,Stoops, B.,Vreeken, R.J.,Vermond, J.,Goutier, W.,Tang, C.,Vogels, R.,Friesen, R.H.E.,Goudsmit, J.,van Dongen, M.J.P.,Wilson, I.A. Potent peptidic fusion inhibitors of influenza virus. Science, 358:496-502, 2017 Cited by PubMed Abstract: Influenza therapeutics with new targets and mechanisms of action are urgently needed to combat potential pandemics, emerging viruses, and constantly mutating strains in circulation. We report here on the design and structural characterization of potent peptidic inhibitors of influenza hemagglutinin. The peptide design was based on complementarity-determining region loops of human broadly neutralizing antibodies against the hemagglutinin (FI6v3 and CR9114). The optimized peptides exhibit nanomolar affinity and neutralization against influenza A group 1 viruses, including the 2009 H1N1 pandemic and avian H5N1 strains. The peptide inhibitors bind to the highly conserved stem epitope and block the low pH-induced conformational rearrangements associated with membrane fusion. These peptidic compounds and their advantageous biological properties should accelerate the development of new small molecule- and peptide-based therapeutics against influenza virus. PubMed: 28971971DOI: 10.1126/science.aan0516 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.461 Å) |
Structure validation
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