2ab9: Difference between revisions

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-[[Image:2ab9.gif|left|200px]]
- {{Structure
+==Discovery, structural determination and processing of the precursor protein that produces the cyclic trypsin inhibitor SFTI-1==
-|PDB= 2ab9 |SIZE=350|CAPTION= <scene name='initialview01'>2ab9</scene>
+<StructureSection load='2ab9' size='340' side='right'caption='[[2ab9]]' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[2ab9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helianthus_annuus Helianthus annuus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AB9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AB9 FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
-|GENE=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ab9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ab9 OCA], [https://pdbe.org/2ab9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ab9 RCSB], [https://www.ebi.ac.uk/pdbsum/2ab9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ab9 ProSAT]</span></td></tr>
-}}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SFTI1_HELAN SFTI1_HELAN] Inhibits trypsin, cathepsin G, elastase, chymotrypsin and thrombin. Does not inhibit factor Xa.<ref>PMID:10390350</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Backbone-cyclized proteins are becoming increasingly well known, although the mechanism by which they are processed from linear precursors is poorly understood. In this report the sequence and structure of the linear precursor of a cyclic trypsin inhibitor, sunflower trypsin inhibitor 1 (SFTI-1) from sunflower seeds, is described. The structure indicates that the major elements of the reactive site loop of SFTI-1 are present before processing. This may have importance for a protease-mediated cyclizing reaction as the rigidity of SFTI-1 may drive the equilibrium of the reaction catalyzed by proteolytic enzymes toward the formation of a peptide bond rather than the normal cleavage reaction. The occurrence of residues in the SFTI-1 precursor susceptible to cleavage by asparaginyl proteases strengthens theories that involve this enzyme in the processing of SFTI-1 and further implicates it in the processing of another family of plant cyclic proteins, the cyclotides. The precursor reported here also indicates that despite strong active site sequence homology, SFTI-1 has no other similarities with the Bowman-Birk trypsin inhibitors, presenting interesting evolutionary questions.
-'''Discovery, structural determination and processing of the precursor protein that produces the cyclic trypsin inhibitor SFTI-1'''
+Discovery, structural determination, and putative processing of the precursor protein that produces the cyclic trypsin inhibitor sunflower trypsin inhibitor 1.,Mulvenna JP, Foley FM, Craik DJ J Biol Chem. 2005 Sep 16;280(37):32245-53. Epub 2005 Jul 21. PMID:16036912<ref>PMID:16036912</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2ab9" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-Backbone-cyclized proteins are becoming increasingly well known, although the mechanism by which they are processed from linear precursors is poorly understood. In this report the sequence and structure of the linear precursor of a cyclic trypsin inhibitor, sunflower trypsin inhibitor 1 (SFTI-1) from sunflower seeds, is described. The structure indicates that the major elements of the reactive site loop of SFTI-1 are present before processing. This may have importance for a protease-mediated cyclizing reaction as the rigidity of SFTI-1 may drive the equilibrium of the reaction catalyzed by proteolytic enzymes toward the formation of a peptide bond rather than the normal cleavage reaction. The occurrence of residues in the SFTI-1 precursor susceptible to cleavage by asparaginyl proteases strengthens theories that involve this enzyme in the processing of SFTI-1 and further implicates it in the processing of another family of plant cyclic proteins, the cyclotides. The precursor reported here also indicates that despite strong active site sequence homology, SFTI-1 has no other similarities with the Bowman-Birk trypsin inhibitors, presenting interesting evolutionary questions.
+*[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-AB9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Helianthus_annuus Helianthus annuus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AB9 OCA].
+__TOC__
+</StructureSection>
-==Reference==
-Discovery, structural determination, and putative processing of the precursor protein that produces the cyclic trypsin inhibitor sunflower trypsin inhibitor 1., Mulvenna JP, Foley FM, Craik DJ, J Biol Chem. 2005 Sep 16;280(37):32245-53. Epub 2005 Jul 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16036912 16036912]
 [[Category: Helianthus annuus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Craik, D J.]]
+[[Category: Craik DJ]]
-[[Category: Foley, F M.]]
+[[Category: Foley FM]]
-[[Category: Mulvenna, J P.]]
+[[Category: Mulvenna JP]]
-[[Category: beta-sheet]]
-[[Category: protein]]
-[[Category: random coil]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:47:45 2008''