View source for 5dz5


==Crystal structure of Dendroaspis polylepis mambalgin-1 wild-type in P41212 space group==
<StructureSection load='5dz5' size='340' side='right'caption='[[5dz5]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5dz5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendroaspis_polylepis_polylepis Dendroaspis polylepis polylepis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DZ5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</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=5dz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dz5 OCA], [https://pdbe.org/5dz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dz5 RCSB], [https://www.ebi.ac.uk/pdbsum/5dz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dz5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/3SX1_DENPO 3SX1_DENPO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mambalgins are peptides isolated from mamba venom that specifically inhibit a set of acid-sensing ion channels (ASICs) to relieve pain. We show here the first full stepwise solid-phase peptide synthesis of mambalgin-1 and confirm the biological activity of the synthetic toxin both in vitro and in vivo. We also report the determination of its 3D crystal structure showing differences with previously described NMR structures. Finally, the functional domain by which the toxin inhibits ASIC1a channels was identified in its loop II and more precisely in the face containing Phe27, Leu32 and Leu34 residues. Moreover, proximity between Leu32 in mambalgin-1 and Phe350 in rASIC1a was proposed from double-mutant cycle analysis. These data give information on the structure and on the pharmacophore for ASIC channel inhibition by mambalgins that could have therapeutic value against pain and probably other neurological disorders.

Mambalgin-1 pain-relieving peptide: stepwise solid-phase synthesis, crystal structure and functional domain for acid-sensing ion channel 1a inhibition.,Mourier G, Salinas M, Kessler P, Stura EA, Leblanc M, Tepshi L, Besson T, Diochot S, Baron A, Douguet D, Lingueglia E, Servent D J Biol Chem. 2015 Dec 17. pii: jbc.M115.702373. PMID:26680001<ref>PMID:26680001</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5dz5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Dendroaspis polylepis polylepis]]
[[Category: Large Structures]]
[[Category: Kessler P]]
[[Category: Mourier G]]
[[Category: Servent D]]
[[Category: Stura EA]]
[[Category: Tepshi L]]