1t54

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|PDB= 1t54 |SIZE=350|CAPTION= <scene name='initialview01'>1t54</scene>
|PDB= 1t54 |SIZE=350|CAPTION= <scene name='initialview01'>1t54</scene>
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|LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene>
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|LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>
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|DOMAIN=
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|RELATEDENTRY=[[1t51|1T51]], [[1t52|1T52]], [[1t55|1T55]]
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1t54 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t54 RCSB]</span>
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[[Category: Lim, S S.]]
[[Category: Lim, S S.]]
[[Category: Shin, S Y.]]
[[Category: Shin, S Y.]]
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[[Category: NH2]]
 
[[Category: coil-helix]]
[[Category: coil-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:13:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:51:24 2008''

Revision as of 20:51, 30 March 2008


PDB ID 1t54

Drag the structure with the mouse to rotate
Ligands:
Related: 1T51, 1T52, 1T55


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

1T54 is a Single protein structure of sequence from Opisthacanthus madagascariensis. Full crystallographic information is available from OCA.

Reference

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

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