2mua: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2mua]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_FC27/Papua_New_Guinea Plasmodium falciparum FC27/Papua New Guinea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MUA FirstGlance]. <br>
<table><tr><td colspan='2'>[[2mua]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_FC27/Papua_New_Guinea Plasmodium falciparum FC27/Papua New Guinea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MUA FirstGlance]. <br>
</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=2mua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mua OCA], [https://pdbe.org/2mua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mua RCSB], [https://www.ebi.ac.uk/pdbsum/2mua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mua ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mua OCA], [https://pdbe.org/2mua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mua RCSB], [https://www.ebi.ac.uk/pdbsum/2mua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mua ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/RESA_PLAFF RESA_PLAFF] May disrupt the normal intermolecular interactions of the cytoplasmic domain of band 3 and thereby facilitate the invagination of the red cell membrane which is necessary for the formation of the parasitophorous vacuole.
[https://www.uniprot.org/uniprot/RESA_PLAFF RESA_PLAFF] May disrupt the normal intermolecular interactions of the cytoplasmic domain of band 3 and thereby facilitate the invagination of the red cell membrane which is necessary for the formation of the parasitophorous vacuole.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
As microbes use many mechanisms for avoiding immunological pressure, new strategies must be developed to bypass the immunological code of silence of conserved, functionally-important amino acid sequences, such as those involved in high activity binding peptides' (HABPs) attaching to their host cells. Hundreds of experiments in large numbers of Aotus monkeys revealed that this immunological code of silence could be broken by shifting the polarity of some critical host cell binding residues in these HABPs by substituting F for R and vice versa, Y&lt;--&gt;W, L&lt;--&gt;H, I&lt;--&gt;N, P&lt;--&gt;D, M&lt;--&gt;K or E, C&lt;--&gt;T, V&lt;--&gt;N or S; there are special rules for A, G and S. (1)H-nuclear magnetic resonance of these modified, immunogenic, protection-inducing HABPs and molecular modelling revealed that such modifications induced appropriate fitting into specific HLA-DRbeta1 Pockets, suggesting the presence of new pockets and a haplotype- and allele-specific conscious TCR. A highly immunogenic and protection-inducing anti-malarial vaccine can thus be produced.
Shifting the polarity of some critical residues in malarial peptides' binding to host cells is a key factor in breaking conserved antigens' code of silence.,Cifuentes G, Bermudez A, Rodriguez R, Patarroyo MA, Patarroyo ME Med Chem. 2008 May;4(3):278-92. PMID:18473921<ref>PMID:18473921</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mua" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
</StructureSection>

Latest revision as of 07:02, 1 May 2024

Shifting the Polarity of some Critical Residues in Malarial Peptides Binding to Host Cells is a Key Factor in Breaking Conserved Antigens

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