2r5d: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Structure of the gp41 N-trimer in complex with the HIV entry inhibitor PIE7== | ==Structure of the gp41 N-trimer in complex with the HIV entry inhibitor PIE7== | ||
<StructureSection load='2r5d' size='340' side='right' caption='[[2r5d]], [[Resolution|resolution]] 1.66Å' scene=''> | <StructureSection load='2r5d' size='340' side='right'caption='[[2r5d]], [[Resolution|resolution]] 1.66Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2r5d]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R5D FirstGlance]. <br> | <table><tr><td colspan='2'>[[2r5d]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R5D FirstGlance]. <br> | ||
| Line 18: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 2r5d" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2r5d" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Gp41 3D Structures|Gp41 3D Structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Heroux, A]] | [[Category: Heroux, A]] | ||
[[Category: Hill, C P]] | [[Category: Hill, C P]] | ||
Revision as of 10:32, 31 July 2019
Structure of the gp41 N-trimer in complex with the HIV entry inhibitor PIE7Structure of the gp41 N-trimer in complex with the HIV entry inhibitor PIE7
Structural highlights
Publication Abstract from PubMedDuring HIV-1 entry, the highly conserved gp41 N-trimer pocket region becomes transiently exposed and vulnerable to inhibition. Using mirror-image phage display and structure-assisted design, we have discovered protease-resistant D-amino acid peptides (D-peptides) that bind the N-trimer pocket with high affinity and potently inhibit viral entry. We also report high-resolution crystal structures of two of these D-peptides in complex with a pocket mimic that suggest sources of their high potency. A trimeric version of one of these peptides is the most potent pocket-specific entry inhibitor yet reported by three orders of magnitude (IC(50) = 250 pM). These results are the first demonstration that D-peptides can form specific and high-affinity interactions with natural protein targets and strengthen their promise as therapeutic agents. The D-peptides described here address limitations associated with current L-peptide entry inhibitors and are promising leads for the prevention and treatment of HIV/AIDS. Potent D-peptide inhibitors of HIV-1 entry.,Welch BD, VanDemark AP, Heroux A, Hill CP, Kay MS Proc Natl Acad Sci U S A. 2007 Oct 23;104(43):16828-33. Epub 2007 Oct 17. PMID:17942675[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||