3mgn
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mgn OCA], [https://pdbe.org/3mgn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mgn RCSB], [https://www.ebi.ac.uk/pdbsum/3mgn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mgn ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mgn OCA], [https://pdbe.org/3mgn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mgn RCSB], [https://www.ebi.ac.uk/pdbsum/3mgn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mgn ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The HIV gp41 N-trimer pocket region is an ideal viral target because it is extracellular, highly conserved, and essential for viral entry. Here, we report on the design of a pocket-specific D-peptide, PIE12-trimer, that is extraordinarily elusive to resistance and characterize its inhibitory and structural properties. D-peptides (peptides composed of D-amino acids) are promising therapeutic agents due to their insensitivity to protease degradation. PIE12-trimer was designed using structure-guided mirror-image phage display and linker optimization and is the first D-peptide HIV entry inhibitor with the breadth and potency required for clinical use. PIE12-trimer has an ultrahigh affinity for the gp41 pocket, providing it with a reserve of binding energy (resistance capacitor) that yields a dramatically improved resistance profile compared to those of other fusion inhibitors. These results demonstrate that the gp41 pocket is an ideal drug target and establish PIE12-trimer as a leading anti-HIV antiviral candidate. | ||
| + | |||
| + | Design of a potent D-peptide HIV-1 entry inhibitor with a strong barrier to resistance.,Welch BD, Francis JN, Redman JS, Paul S, Weinstock MT, Reeves JD, Lie YS, Whitby FG, Eckert DM, Hill CP, Root MJ, Kay MS J Virol. 2010 Nov;84(21):11235-44. Epub 2010 Aug 18. PMID:20719956<ref>PMID:20719956</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3mgn" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
D-Peptide inhibitor PIE71 in complex with IQN17
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Categories: Large Structures | Francis N | Hill CP | Kay M | Whitby FG
