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| - | [[Image:1iyc.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1iyc| PDB=1iyc | SCENE= }} | | {{STRUCTURE_1iyc| PDB=1iyc | SCENE= }} |
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| - | '''Solution structure of antifungal peptide, scarabaecin'''
| + | ===Solution structure of antifungal peptide, scarabaecin=== |
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| - | ==Overview==
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| - | Scarabaecin isolated from hemolymph of the coconut rhinoceros beetle Oryctes rhinoceros is a 36-residue polypeptide that has antifungal activity. The solution structure of scarabaecin has been determined from twodimensional 1H NMR spectroscopic data and hybrid distance geometry-simulated annealing protocol calculation. Based on 492 interproton and 10 hydrogen-bonding distance restraints and 36 dihedral angle restraints, we obtained 20 structures. The average backbone root-mean-square deviation for residues 4-35 is 0.728 +/- 0.217 A from the mean structure. The solution structure consists of a two-stranded antiparallel beta-sheet connected by a type-I beta-turn after a short helical turn. All secondary structures and a conserved disulfide bond are located in the C-terminal half of the peptide, residues 18-36. Overall folding is stabilized by a combination of a disulfide bond, seven hydrogen bonds, and numerous hydrophobic interactions. The structural motif of the C-terminal half shares a significant tertiary structural similarity with chitin-binding domains of plant and invertebrate chitin-binding proteins, even though scarabaecin has no overall sequence similarity to other peptide/polypeptides including chitin-binding proteins. The length of its primary structure, the number of disulfide bonds, and the pattern of conserved functional residues binding to chitin in scarabaecin differ from those of chitin-binding proteins in other invertebrates and plants, suggesting that scarabaecin does not share a common ancestor with them. These results are thought to provide further strong experimental evidence to the hypothesis that chitin-binding proteins of invertebrates and plants are correlated by a convergent evolution process.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12676931}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12676931 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12676931}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1IYC is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYC OCA]. | + | 1IYC is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYC OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Chitin-binding]] | | [[Category: Chitin-binding]] |
| | [[Category: Nmr]] | | [[Category: Nmr]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:34:41 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:12:54 2008'' |
Revision as of 11:12, 1 July 2008
Template:STRUCTURE 1iyc
Solution structure of antifungal peptide, scarabaecin
Template:ABSTRACT PUBMED 12676931
About this Structure
1IYC is a Single protein structure. Full experimental information is available from OCA.
Reference
Structural basis for new pattern of conserved amino acid residues related to chitin-binding in the antifungal peptide from the coconut rhinoceros beetle Oryctes rhinoceros., Hemmi H, Ishibashi J, Tomie T, Yamakawa M, J Biol Chem. 2003 Jun 20;278(25):22820-7. Epub 2003 Apr 3. PMID:12676931
Page seeded by OCA on Tue Jul 1 14:12:54 2008
