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| - | [[Image:1ju8.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ju8| PDB=1ju8 | SCENE= }} | | {{STRUCTURE_1ju8| PDB=1ju8 | SCENE= }} |
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| - | '''Solution structure of Leginsulin, a plant hormon'''
| + | ===Solution structure of Leginsulin, a plant hormon=== |
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| - | ==Overview==
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| - | Previously, we isolated a 4-kDa peptide capable of binding to a 43-kDa receptor-like protein and stimulating protein kinase activity of the 43-kDa protein in soybean. Both of them were found to localize in the plasma membranes and cell walls. Here, we report the physiological effects of 4-kDa peptide expressed transiently in the cultured carrot and bird's-foot trefoil cells transfected with pBI 121 plasmid containing the 4-kDa peptide gene. At early developmental stage, the transgenic callus grew rapidly compared to the wild callus in both species. Cell proliferation of in vitro cultured nonembryogenic carrot callus was apparently affected with the 4-kDa peptide in the medium. Complementary DNAs encoding the 4-kDa peptide from mung bean and azuki bean were cloned by PCR and sequenced. The amino-acid sequences deduced from the nucleotide sequences are homologous among legume species, particularly, the sites of cysteine residues are highly conserved. This conserved sequence reflects the importance of intradisulfide bonds required for the 4-kDa peptide to perform its function. Three dimensional structure of the 4-kDa peptide determined by NMR spectroscopy suggests that this peptide is a T-knot scaffold containing three beta-strands, and the specific binding activity to the 43-kDa protein and stimulatory effect on the protein phosphorylation could be attributed to the spatial arrangements of hydrophobic residues at the solvent-exposed surface of two-stranded beta-sheet of 4-kDa peptide. The importance of these residues for the 4-kDa peptide to bind to the 43-kDa protein was indicated by site-directed mutagenesis. These results suggest that the 4-kDa peptide is a hormone-like peptide and the 43-kDa protein is involved in cellular signal transduction of the peptide.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12631285}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12631285 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12631285}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1JU8 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JU8 OCA]. | + | 1JU8 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JU8 OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Yamazaki, T.]] | | [[Category: Yamazaki, T.]] |
| | [[Category: T-knot]] | | [[Category: T-knot]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:55:53 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:53:00 2008'' |
Revision as of 17:53, 1 July 2008
Template:STRUCTURE 1ju8
Solution structure of Leginsulin, a plant hormon
Template:ABSTRACT PUBMED 12631285
About this Structure
1JU8 is a Single protein structure. Full experimental information is available from OCA.
Reference
A possible physiological function and the tertiary structure of a 4-kDa peptide in legumes., Yamazaki T, Takaoka M, Katoh E, Hanada K, Sakita M, Sakata K, Nishiuchi Y, Hirano H, Eur J Biochem. 2003 Mar;270(6):1269-76. PMID:12631285
Page seeded by OCA on Tue Jul 1 20:53:00 2008
