1kfp
From Proteopedia
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| - | [[Image:1kfp.gif|left|200px]] | ||
| - | + | ==Solution structure of the antimicrobial 18-residue gomesin== | |
| - | + | <StructureSection load='1kfp' size='340' side='right'caption='[[1kfp]]' scene=''> | |
| - | | | + | == Structural highlights == |
| - | | | + | <table><tr><td colspan='2'>[[1kfp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acanthoscurria_gomesiana Acanthoscurria gomesiana]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1KFP FirstGlance]. <br> |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=1kfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfp OCA], [https://pdbe.org/1kfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfp RCSB], [https://www.ebi.ac.uk/pdbsum/1kfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfp ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | ''' | + | == Function == |
| - | + | [https://www.uniprot.org/uniprot/GOME_ACAGO 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.<ref>PMID:10942757</ref> | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | == | + | == 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. | 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<ref>PMID:11856345</ref> | |
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| - | The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider., Mandard N, Bulet P, Caille A, Daffre S, Vovelle F | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 1kfp" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Acanthoscurria gomesiana]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bulet P]] | ||
| + | [[Category: Caille A]] | ||
| + | [[Category: Daffre S]] | ||
| + | [[Category: Mandard N]] | ||
| + | [[Category: Vovelle F]] | ||
Current revision
Solution structure of the antimicrobial 18-residue gomesin
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