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| | ==Crystal structure of recombinant Kunitz Type serine protease Inhibitor-1 from the Carribean sea anemone stichodactyla helianthus== | | ==Crystal structure of recombinant Kunitz Type serine protease Inhibitor-1 from the Carribean sea anemone stichodactyla helianthus== |
| - | <StructureSection load='3ofw' size='340' side='right' caption='[[3ofw]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='3ofw' size='340' side='right'caption='[[3ofw]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ofw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Stichodactyla_helianthus Stichodactyla helianthus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OFW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OFW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ofw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Stichodactyla_helianthus Stichodactyla helianthus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OFW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3m7q|3m7q]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ofw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ofw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ofw RCSB], [http://www.ebi.ac.uk/pdbsum/3ofw PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ofw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ofw OCA], [https://pdbe.org/3ofw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ofw RCSB], [https://www.ebi.ac.uk/pdbsum/3ofw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ofw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/VKT1_STIHL VKT1_STIHL] Active against serine, cysteine, and aspartic proteases. Can bind vertebrate trypsin and chymotrypsin.<ref>PMID:22975140</ref> <ref>PMID:9027993</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3ofw" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Stichodactyla helianthus]] | | [[Category: Stichodactyla helianthus]] |
| - | [[Category: Betzel, C]] | + | [[Category: Betzel C]] |
| - | [[Category: Chavez, M de los Angeles]]
| + | [[Category: Garcia-Fernandez R]] |
| - | [[Category: Garcia-Fernandez, R]] | + | [[Category: Gil D]] |
| - | [[Category: Gil, D]] | + | [[Category: Gonzalez Y]] |
| - | [[Category: Gonzalez, Y]] | + | [[Category: Perbandt M]] |
| - | [[Category: Perbandt, M]] | + | [[Category: Pons T]] |
| - | [[Category: Pons, T]] | + | [[Category: Redecke L]] |
| - | [[Category: Redecke, L]] | + | [[Category: Talavera A]] |
| - | [[Category: Talavera, A]] | + | [[Category: De los Angeles Chavez M]] |
| - | [[Category: Hydrolase-hydrolase inhibitor complex]] | + | |
| - | [[Category: Kunitz type]]
| + | |
| - | [[Category: Serine protease]]
| + | |
| - | [[Category: Serine protease inhibitor]]
| + | |
| Structural highlights
Function
VKT1_STIHL Active against serine, cysteine, and aspartic proteases. Can bind vertebrate trypsin and chymotrypsin.[1] [2]
Publication Abstract from PubMed
The BPTI/Kunitz-type inhibitor family includes several extremely potent serine protease inhibitors. To date, the inhibitory mechanisms have only been studied for mammalian inhibitors. Here, the first crystal structure of a BPTI/Kunitz-type inhibitor from a marine invertebrate (rShPI-1A) is reported to 2.5 A resolution. Crystallization of recombinant rShPI-1A required the salt-induced dissociation of a trypsin complex that was previously formed to avoid intrinsic inhibitor aggregates in solution. The rShPI-1A structure is similar to the NMR structure of the molecule purified from the natural source, but allowed the assignment of disulfide-bridge chiralities and the detection of an internal stabilizing water network. A structural comparison with other BPTI/Kunitz-type canonical inhibitors revealed unusual varphi angles at positions 17 and 30 to be a particular characteristic of the family. A significant clustering of varphi and psi angle values in the glycine-rich remote fragment near the secondary binding loop was additionally identified, but its impact on the specificity of rShPI-1A and similar molecules requires further study.
Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the marine invertebrate Stichodactyla helianthus.,Garcia-Fernandez R, Pons T, Meyer A, Perbandt M, Gonzalez-Gonzalez Y, Gil D, de los Angeles Chavez M, Betzel C, Redecke L Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Nov 1;68(Pt 11):1289-93., doi: 10.1107/S1744309112039085. Epub 2012 Oct 26. PMID:23143234[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Garcia-Fernandez R, Pons T, Perbandt M, Valiente PA, Talavera A, Gonzalez-Gonzalez Y, Rehders D, Chavez MA, Betzel C, Redecke L. Structural insights into serine protease inhibition by a marine invertebrate BPTI Kunitz-type inhibitor. J Struct Biol. 2012 Sep 5. pii: S1047-8477(12)00240-7. doi:, 10.1016/j.jsb.2012.08.009. PMID:22975140 doi:http://dx.doi.org/10.1016/j.jsb.2012.08.009
- ↑ Delfin J, Martinez I, Antuch W, Morera V, Gonzalez Y, Rodriguez R, Marquez M, Saroyan A, Larionova N, Diaz J, Padron G, Chavez M. Purification, characterization and immobilization of proteinase inhibitors from Stichodactyla helianthus. Toxicon. 1996 Nov-Dec;34(11-12):1367-76. PMID:9027993
- ↑ Garcia-Fernandez R, Pons T, Meyer A, Perbandt M, Gonzalez-Gonzalez Y, Gil D, de los Angeles Chavez M, Betzel C, Redecke L. Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the marine invertebrate Stichodactyla helianthus. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Nov 1;68(Pt 11):1289-93., doi: 10.1107/S1744309112039085. Epub 2012 Oct 26. PMID:23143234 doi:http://dx.doi.org/10.1107/S1744309112039085
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