2e2f: Difference between revisions
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< | ==Solution structure of DSP== | ||
<StructureSection load='2e2f' size='340' side='right'caption='[[2e2f]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2e2f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gastrophysa_atrocyanea Gastrophysa atrocyanea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E2F FirstGlance]. <br> | |||
</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=2e2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e2f OCA], [https://pdbe.org/2e2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e2f RCSB], [https://www.ebi.ac.uk/pdbsum/2e2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e2f ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DIAP_GASAT DIAP_GASAT] Has antifungal activity against T.rubrum. Blocks voltage-dependent N-type calcium channels (Cav2.2 / CACNA1B).<ref>PMID:14706547</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Diapause-specific peptide (DSP), derived from the leaf beetle, inhibits Ca2+ channels and has antifungal activity. DSP acts on chromaffin cells of the adrenal medulla in a fashion similar to that of omega-conotoxin GVIA, a well-known neurotoxic peptide, and blocks N-type voltage-dependent Ca2+ channels. However, the amino acid sequence of DSP has little homology with any other known Ca2+ channel blockers or antifungal peptides. In this paper, we analyzed the solution structure of DSP by using two-dimensional 1H nuclear magnetic resonance and determined the pairing of half-cystine residues forming disulfide bonds. The arrangement of the three disulfide bridges in DSP was distinct from that of other antifungal peptides and conotoxins. The overall structure of DSP is compact due in part to the three disulfide bridges and, interestingly, is very similar to those of the insect- and plant-derived antifungal peptides. On the other hand, the disulfide arrangement and the three-dimensional structure of DSP and GVIA are not similar. Nevertheless, some surface residues of DSP superimpose on the key functional residues of GVIA. This homologous distribution of hydrophobic and charged side chains may result in the functional similarity between DSP and GVIA. Thus, we propose here that the three-dimensional structure of DSP can explain its dual function as a Ca2+ channel blocker and antifungal peptide. | |||
The structure of a novel insect peptide explains its Ca2+ channel blocking and antifungal activities.,Kouno T, Mizuguchi M, Tanaka H, Yang P, Mori Y, Shinoda H, Unoki K, Aizawa T, Demura M, Suzuki K, Kawano K Biochemistry. 2007 Dec 4;46(48):13733-41. Epub 2007 Nov 10. PMID:17994764<ref>PMID:17994764</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2e2f" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
[[Category: Gastrophysa atrocyanea]] | [[Category: Gastrophysa atrocyanea]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Kawano | [[Category: Kawano K]] | ||
[[Category: Kouno | [[Category: Kouno T]] | ||
[[Category: Mizuguchi | [[Category: Mizuguchi M]] | ||
[[Category: Suzuki | [[Category: Suzuki K]] | ||
Latest revision as of 08:34, 15 May 2024
Solution structure of DSPSolution structure of DSP
Structural highlights
FunctionDIAP_GASAT Has antifungal activity against T.rubrum. Blocks voltage-dependent N-type calcium channels (Cav2.2 / CACNA1B).[1] Publication Abstract from PubMedDiapause-specific peptide (DSP), derived from the leaf beetle, inhibits Ca2+ channels and has antifungal activity. DSP acts on chromaffin cells of the adrenal medulla in a fashion similar to that of omega-conotoxin GVIA, a well-known neurotoxic peptide, and blocks N-type voltage-dependent Ca2+ channels. However, the amino acid sequence of DSP has little homology with any other known Ca2+ channel blockers or antifungal peptides. In this paper, we analyzed the solution structure of DSP by using two-dimensional 1H nuclear magnetic resonance and determined the pairing of half-cystine residues forming disulfide bonds. The arrangement of the three disulfide bridges in DSP was distinct from that of other antifungal peptides and conotoxins. The overall structure of DSP is compact due in part to the three disulfide bridges and, interestingly, is very similar to those of the insect- and plant-derived antifungal peptides. On the other hand, the disulfide arrangement and the three-dimensional structure of DSP and GVIA are not similar. Nevertheless, some surface residues of DSP superimpose on the key functional residues of GVIA. This homologous distribution of hydrophobic and charged side chains may result in the functional similarity between DSP and GVIA. Thus, we propose here that the three-dimensional structure of DSP can explain its dual function as a Ca2+ channel blocker and antifungal peptide. The structure of a novel insect peptide explains its Ca2+ channel blocking and antifungal activities.,Kouno T, Mizuguchi M, Tanaka H, Yang P, Mori Y, Shinoda H, Unoki K, Aizawa T, Demura M, Suzuki K, Kawano K Biochemistry. 2007 Dec 4;46(48):13733-41. Epub 2007 Nov 10. PMID:17994764[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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