1kfp
From Proteopedia
(New page: 200px<br /><applet load="1kfp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kfp" /> '''Solution structure of the antimicrobial 18-r...) |
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'''Solution structure of the antimicrobial 18-residue gomesin'''<br /> | '''Solution structure of the antimicrobial 18-residue gomesin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Gomesin is the first peptide isolated from spider exhibiting antimicrobial | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1KFP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1KFP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hairpin-like]] | [[Category: hairpin-like]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:40 2008'' |
Revision as of 11:33, 21 February 2008
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Solution structure of the antimicrobial 18-residue gomesin
Overview
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.
About this Structure
1KFP is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 13:33:40 2008
