4mzk: Difference between revisions
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==Crystal Structure of MTIP from Plasmodium falciparum in complex with pGly[807,811], a stapled myoA tail peptide== | ==Crystal Structure of MTIP from Plasmodium falciparum in complex with pGly[807,811], a stapled myoA tail peptide== | ||
<StructureSection load='4mzk' size='340' side='right' caption='[[4mzk]], [[Resolution|resolution]] 1.82Å' scene=''> | <StructureSection load='4mzk' size='340' side='right' caption='[[4mzk]], [[Resolution|resolution]] 1.82Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4aom|4aom]], [[4mzj|4mzj]], [[4mzl|4mzl]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4aom|4aom]], [[4mzj|4mzj]], [[4mzl|4mzl]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MTIP, PFL2225w ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MTIP, PFL2225w ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mzk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mzk RCSB], [http://www.ebi.ac.uk/pdbsum/4mzk PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mzk OCA], [http://pdbe.org/4mzk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mzk RCSB], [http://www.ebi.ac.uk/pdbsum/4mzk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mzk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4mzk" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 20:50, 4 August 2016
Crystal Structure of MTIP from Plasmodium falciparum in complex with pGly[807,811], a stapled myoA tail peptideCrystal Structure of MTIP from Plasmodium falciparum in complex with pGly[807,811], a stapled myoA tail peptide
Structural highlights
Function[MYOA_PLAF7] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). Publication Abstract from PubMedConstrained alpha-helical peptides are an exciting class of molecule designed to disrupt protein-protein interactions (PPIs) at a surface-exposed helix binding site. Complexes that engage more than one helical face account for over a third of structurally characterized helix PPIs, including several examples where the helix is fully buried. However, no constrained peptides have been reported that have targeted this class of interaction. We report the design of stapled and hydrogen bond surrogate (HBS) peptides mimicking the helical tail of the malaria parasite invasion motor myosin (myoA), which presents polar and hydrophobic functionality on all three faces in binding its partner, myoA tail interacting protein (MTIP), with high affinity. The first structures of these different constrained peptides bound to the same target are reported, enabling a direct comparison between these constraints and between staples based on monosubstituted pentenyl glycine (pGly) and disubstituted pentenyl alanine (pAla). Importantly, installation of these constraints does not disrupt native interactions in the buried site, so the affinity of the wild-type peptide is maintained. Crystal Structures of Stapled and Hydrogen Bond Surrogate Peptides Targeting a Fully Buried Protein-Helix Interaction.,Douse CH, Maas SJ, Thomas JC, Garnett JA, Sun Y, Cota E, Tate EW ACS Chem Biol. 2014 Aug 6. PMID:25084543[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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