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1kfp

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Revision as of 07:32, 11 October 2017

Solution structure of the antimicrobial 18-residue gomesin

Structural highlights

1kfp is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GOME_ACAGO] Active against several Gram-positive bacteria such as Bacillus spp, Staphylococcus spp and E.faecalis, several Gram-negative bacteria such as E.coli, K.pneumoniae, P.aeruginosa and Salmonella spp, filamentous fungi such as N.crassa, T.viridae and yeasts such as C.albicans. It is active against the parasite L.amazonensis as well. It shows hemolytic activity.^[1]

Publication Abstract from PubMed

Gomesin is the first peptide isolated from spider exhibiting antimicrobial activities. This highly cationic peptide is composed of 18 amino-acid residues including four cysteines forming two disulfide linkages. The solution structure of gomesin has been determined using proton two-dimensional NMR (2D-NMR) and restrained molecular dynamics calculations. The global fold of gomesin consists in a well-resolved two-stranded antiparallel betasheet connected by a noncanonical betaturn. A comparison between the structures of gomesin and protegrin-1 from porcine and androctonin from scorpion outlines several common features in the distribution of hydrophobic and hydrophilic residues. The N- and C-termini, the betaturn and one face of the betasheet are hydrophilic, but the hydrophobicity of the other face depends on the peptide. The similarities suggest that the molecules interact with membranes in an analogous manner. The importance of the intramolecular disulfide bridges in the biological activity of gomesin is being investigated.

The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider.,Mandard N, Bulet P, Caille A, Daffre S, Vovelle F Eur J Biochem. 2002 Feb;269(4):1190-8. PMID:11856345^[2]

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

References

↑ Silva PI Jr, Daffre S, Bulet P. Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family. J Biol Chem. 2000 Oct 27;275(43):33464-70. PMID:10942757 doi:http://dx.doi.org/10.1074/jbc.M001491200
↑ Mandard N, Bulet P, Caille A, Daffre S, Vovelle F. The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider. Eur J Biochem. 2002 Feb;269(4):1190-8. PMID:11856345

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/1kfp"

@@ Line 1: / Line 1: @@
 ==Solution structure of the antimicrobial 18-residue gomesin==
 <StructureSection load='1kfp' size='340' side='right' caption='[[1kfp]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1kfp]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFP FirstGlance]. <br>
 </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>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=1kfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfp OCA], [http://pdbe.org/1kfp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kfp RCSB], [http://www.ebi.ac.uk/pdbsum/1kfp 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=1kfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfp OCA], [http://pdbe.org/1kfp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kfp RCSB], [http://www.ebi.ac.uk/pdbsum/1kfp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfp ProSAT]</span></td></tr>
 </table>
 == Function ==

1kfp

From Proteopedia

Revision as of 07:32, 11 October 2017

Solution structure of the antimicrobial 18-residue gomesin

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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