1sfi: Difference between revisions
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[[Image:1sfi.gif|left|200px]]<br /><applet load="1sfi" size=" | [[Image:1sfi.gif|left|200px]]<br /><applet load="1sfi" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1sfi, resolution 1.65Å" /> | caption="1sfi, resolution 1.65Å" /> | ||
'''HIGH RESOLUTION STRUCTURE OF A POTENT, CYCLIC PROTEASE INHIBITOR FROM SUNFLOWER SEEDS'''<br /> | '''HIGH RESOLUTION STRUCTURE OF A POTENT, CYCLIC PROTEASE INHIBITOR FROM SUNFLOWER SEEDS'''<br /> | ||
==Overview== | ==Overview== | ||
Proteinaceous serine proteinase inhibitors are widespread throughout the | Proteinaceous serine proteinase inhibitors are widespread throughout the plant kingdom where they play an important role in protection against pests and pathogens. Here, we describe the isolation and characterisation of a novel 14 amino acid residue cyclic peptide from sunflower seeds, which is a potent inhibitor of trypsin (Ki=100 pM). The crystal structure of this peptide in complex with bovine beta-trypsin shows both sequence and conformational similarity with the trypsin-reactive loop of the Bowman-Birk family of serine proteinase inhibitors. This inhibitor, however, is unique in being monofunctional, cyclic and far shorter (14 amino acid residues) than inhibitors belonging to this family (typically 60-70 amino acid residues). The high potency of this peptide is likely to arise from the considerable structural rigidity achieved through its cyclic nature which is further stabilised by a single internal disulphide bond. This study helps delineate the minimal unit required for effective peptide inhibitors of serine proteinases, and will assist in the further design of inhibitors to this widespread class of enzymes. | ||
==About this Structure== | ==About this Structure== | ||
1SFI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Helianthus_annuus Helianthus annuus] with SO4 and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http:// | 1SFI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Helianthus_annuus Helianthus annuus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SFI OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Trypsin]] | [[Category: Trypsin]] | ||
[[Category: Barker, J | [[Category: Barker, J J.]] | ||
[[Category: Brady, R | [[Category: Brady, R L.]] | ||
[[Category: Clarke, A | [[Category: Clarke, A R.]] | ||
[[Category: Garcia, R | [[Category: Garcia, R S.]] | ||
[[Category: Konarev, A | [[Category: Konarev, A V.]] | ||
[[Category: Luckett, S.]] | [[Category: Luckett, S.]] | ||
[[Category: Shewry, P.]] | [[Category: Shewry, P.]] | ||
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[[Category: trypsin inhibitor]] | [[Category: trypsin inhibitor]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:56 2008'' | ||
Revision as of 16:00, 21 February 2008
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HIGH RESOLUTION STRUCTURE OF A POTENT, CYCLIC PROTEASE INHIBITOR FROM SUNFLOWER SEEDS
OverviewOverview
Proteinaceous serine proteinase inhibitors are widespread throughout the plant kingdom where they play an important role in protection against pests and pathogens. Here, we describe the isolation and characterisation of a novel 14 amino acid residue cyclic peptide from sunflower seeds, which is a potent inhibitor of trypsin (Ki=100 pM). The crystal structure of this peptide in complex with bovine beta-trypsin shows both sequence and conformational similarity with the trypsin-reactive loop of the Bowman-Birk family of serine proteinase inhibitors. This inhibitor, however, is unique in being monofunctional, cyclic and far shorter (14 amino acid residues) than inhibitors belonging to this family (typically 60-70 amino acid residues). The high potency of this peptide is likely to arise from the considerable structural rigidity achieved through its cyclic nature which is further stabilised by a single internal disulphide bond. This study helps delineate the minimal unit required for effective peptide inhibitors of serine proteinases, and will assist in the further design of inhibitors to this widespread class of enzymes.
About this StructureAbout this Structure
1SFI is a Single protein structure of sequence from Bos taurus and Helianthus annuus with and as ligands. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
ReferenceReference
High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds., Luckett S, Garcia RS, Barker JJ, Konarev AV, Shewry PR, Clarke AR, Brady RL, J Mol Biol. 1999 Jul 9;290(2):525-33. PMID:10390350
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