This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1t54

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:57, 14 March 2018

Antibiotic Activity and Structural Analysis of a Scorpion-derived Antimicrobial peptide IsCT and Its Analogs

Structural highlights

1t54 is a 1 chain structure with sequence from Opima. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1t51, 1t52, 1t55
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NDB52_OPIMA] Cytotoxic linear peptide IsCT: shows weak hemolytic activity and antibacterial activity against both Gram-positive and Gram-negative bacteria probably by forming pores in the cell membrane. IsCT adopts an amphipathic alpha-helical structure. Cytotoxic linear peptide IsCTf: shows neither hemolytic, nor antibacterial activities, probably because it cannot adopt amphipathic alpha-helical structure.

Publication Abstract from PubMed

IsCT is a non-cell-selective antimicrobial peptide isolated from the scorpion Opisthacanthus madagascariensis that has potent cytolytic activity against both mammalian and bacterial cells. To investigate the structure-activity relationships of IsCT and to design novel peptide antibiotics with bacterial cell selectivity, we synthesized several analogs of IsCT and determined their three-dimensional structures in solution by 2D-NMR spectroscopy. IsCT has a linear alpha-helical structure from Gly3 to Phe13, and [K7]-IsCT has a linear alpha-helical structure from Leu2 to Phe13. [K7, P8, K11]-IsCT, which has a bend in its middle region, exhibited the highest antibacterial activity without hemolytic activity, suggesting that its proline-induced bend is an important determinant of this selectivity. Tryptophan fluorescence showed that the high selectivity of [K7, P8, K11]-IsCT toward bacterial cells is closely correlated with its highly selective interaction with negatively charged phospholipids. Its potent activity against antibiotic-resistant bacteria suggests that [K7, P8, K11]-IsCT may serve as a promising lead candidate in the development of new peptide antibiotics.

Antibiotic activity and structural analysis of the scorpion-derived antimicrobial peptide IsCT and its analogs.,Lee K, Shin SY, Kim K, Lim SS, Hahm KS, Kim Y Biochem Biophys Res Commun. 2004 Oct 15;323(2):712-9. PMID:15369808^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lee K, Shin SY, Kim K, Lim SS, Hahm KS, Kim Y. Antibiotic activity and structural analysis of the scorpion-derived antimicrobial peptide IsCT and its analogs. Biochem Biophys Res Commun. 2004 Oct 15;323(2):712-9. PMID:15369808 doi:10.1016/j.bbrc.2004.08.144

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1t54"

@@ Line 1: / Line 1: @@
 ==Antibiotic Activity and Structural Analysis of a Scorpion-derived Antimicrobial peptide IsCT and Its Analogs==
 <StructureSection load='1t54' size='340' side='right' caption='[[1t54]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t51|1t51]], [[1t52|1t52]], [[1t55|1t55]]</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=1t54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t54 OCA], [http://pdbe.org/1t54 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t54 RCSB], [http://www.ebi.ac.uk/pdbsum/1t54 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=1t54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t54 OCA], [http://pdbe.org/1t54 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t54 RCSB], [http://www.ebi.ac.uk/pdbsum/1t54 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t54 ProSAT]</span></td></tr>
 </table>
 == Function ==

1t54

From Proteopedia

Revision as of 07:57, 14 March 2018

Antibiotic Activity and Structural Analysis of a Scorpion-derived Antimicrobial peptide IsCT and Its Analogs

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox