From Proteopedia
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| | {{STRUCTURE_1jbn| PDB=1jbn | SCENE= }} | | {{STRUCTURE_1jbn| PDB=1jbn | SCENE= }} |
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| - | '''SOLUTION STUCTURE OF AN ACYCLIC PERMUTANT OF SFTI-1, A TRYPSIN INHIBITOR FROM SUNFLOWER SEEDS'''
| + | ===SOLUTION STUCTURE OF AN ACYCLIC PERMUTANT OF SFTI-1, A TRYPSIN INHIBITOR FROM SUNFLOWER SEEDS=== |
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| - | ==Overview==
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| - | SFTI-1 is a recently discovered cyclic peptide trypsin inhibitor from sunflower seeds comprising 14 amino acid residues. It is the most potent known Bowman-Birk inhibitor and the only naturally occurring cyclic one. The solution structure of SFTI-1 has been determined by 1H-NMR spectroscopy and compared with a synthetic acyclic permutant. The solution structures of both are remarkably similar. The lowest energy structures from each family of 20 structures of cyclic and acyclic SFTI-1 have an rmsd over the backbone and heavy atoms of 0.29 A and 0.66 A, respectively. The structures consist of two short antiparallel beta-strands joined by an extended loop containing the active site at one end. Cyclic SFTI-1 also has a hairpin turn completing the cycle. Both molecules contain particularly stable arrangements of cross-linking hydrogen bonds between the beta-strands and a single disulfide bridge, making them rigid and well defined in solution. These stable arrangements allow both the cyclic and acyclic variants of SFTI-1 to inhibit trypsin with very high potencies (0.5 nM and 12.1 nM, respectively). The cyclic nature of SFTI-1 appears to have evolved to provide higher trypsin inhibition as well as higher stability. The solution structures are similar to the crystal structure of the cyclic inhibitor in complex with trypsin. The lack of a major conformational change upon binding suggests that the structure of SFTI-1 is rigid and already pre-organized for maximal binding due to minimization of entropic losses compared to a more flexible ligand. These properties make SFTI-1 an ideal platform for the design of small peptidic pharmaceuticals or pesticides.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11493011}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11493011 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11493011}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1JBN is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JBN OCA]. | + | 1JBN is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JBN OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Beta sheet]] | | [[Category: Beta sheet]] |
| | [[Category: Linear backbone]] | | [[Category: Linear backbone]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:01:24 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 19:58:55 2008'' |
Revision as of 16:58, 1 July 2008
Template:STRUCTURE 1jbn
SOLUTION STUCTURE OF AN ACYCLIC PERMUTANT OF SFTI-1, A TRYPSIN INHIBITOR FROM SUNFLOWER SEEDS
Template:ABSTRACT PUBMED 11493011
About this Structure
1JBN is a Single protein structure. Full experimental information is available from OCA.
Reference
Solution structures by 1H NMR of the novel cyclic trypsin inhibitor SFTI-1 from sunflower seeds and an acyclic permutant., Korsinczky ML, Schirra HJ, Rosengren KJ, West J, Condie BA, Otvos L, Anderson MA, Craik DJ, J Mol Biol. 2001 Aug 17;311(3):579-91. PMID:11493011
Page seeded by OCA on Tue Jul 1 19:58:55 2008
