1kfp
From Proteopedia
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|PDB= 1kfp |SIZE=350|CAPTION= <scene name='initialview01'>1kfp</scene> | |PDB= 1kfp |SIZE=350|CAPTION= <scene name='initialview01'>1kfp</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | + | |LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<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://www.ebi.ac.uk/pdbsum/1kfp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kfp RCSB]</span> | ||
}} | }} | ||
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[[Category: Mandard, N.]] | [[Category: Mandard, N.]] | ||
[[Category: Vovelle, F.]] | [[Category: Vovelle, F.]] | ||
| - | [[Category: NH2]] | ||
[[Category: beta-sheet]] | [[Category: beta-sheet]] | ||
[[Category: disulfide bridge]] | [[Category: disulfide bridge]] | ||
[[Category: hairpin-like]] | [[Category: hairpin-like]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:47:56 2008'' |
Revision as of 18:47, 30 March 2008
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. 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
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