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==SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGCI[L30R, K31M]== | |||
<StructureSection load='1kio' size='340' side='right'caption='[[1kio]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1kio]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schistocerca_gregaria Schistocerca gregaria]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KIO FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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=1kio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kio OCA], [https://pdbe.org/1kio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kio RCSB], [https://www.ebi.ac.uk/pdbsum/1kio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kio ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SGP1_SCHGR SGP1_SCHGR] In vitro, SGPI-1/SGCI is active against alpha-chymotrypsin and trypsin while SGPI-2/SGTI is active against alpha-chymotrypsin and pancreatic elastase. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
== | |||
The solution structure of three small serine proteinase inhibitors, two natural and one engineered protein, SGCI (Schistocerca gregaria chymotrypsin inhibitor), SGCI[L30R, K31M] and SGTI (Schistocerca gregaria trypsin inhibitor), were determined by homonuclear NMR-spectroscopy. The molecules exhibit different specificities towards target proteinases, where SGCI is a good chymotrypsin inhibitor, its mutant is a potent trypsin inhibitor, and SGTI inhibits both proteinases weakly. Interestingly, SGTI is a much better inhibitor of insect proteinases than of the mammalian ones used in common assays. All three molecules have a similar fold composed from three antiparallel beta-pleated sheets with three disulfide bridges. The proteinase binding loop has a somewhat distinct geometry in all three peptides. Moreover, the stabilization of the structure is different in SGCI and SGTI. Proton-deuterium exchange experiments are indicative of a highly rigid core in SGTI but not in SGCI. We suggest that the observed structural properties play a significant role in the specificity of these inhibitors. | The solution structure of three small serine proteinase inhibitors, two natural and one engineered protein, SGCI (Schistocerca gregaria chymotrypsin inhibitor), SGCI[L30R, K31M] and SGTI (Schistocerca gregaria trypsin inhibitor), were determined by homonuclear NMR-spectroscopy. The molecules exhibit different specificities towards target proteinases, where SGCI is a good chymotrypsin inhibitor, its mutant is a potent trypsin inhibitor, and SGTI inhibits both proteinases weakly. Interestingly, SGTI is a much better inhibitor of insect proteinases than of the mammalian ones used in common assays. All three molecules have a similar fold composed from three antiparallel beta-pleated sheets with three disulfide bridges. The proteinase binding loop has a somewhat distinct geometry in all three peptides. Moreover, the stabilization of the structure is different in SGCI and SGTI. Proton-deuterium exchange experiments are indicative of a highly rigid core in SGTI but not in SGCI. We suggest that the observed structural properties play a significant role in the specificity of these inhibitors. | ||
Comparative structure analysis of proteinase inhibitors from the desert locust, Schistocerca gregaria.,Gaspari Z, Patthy A, Graf L, Perczel A Eur J Biochem. 2002 Jan;269(2):527-37. PMID:11856311<ref>PMID:11856311</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1kio" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Chymotrypsin inhibitor 3D structures|Chymotrypsin inhibitor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Schistocerca gregaria]] | |||
[[Category: Gaspari Z]] | |||
[[Category: Graf L]] | |||
[[Category: Patthy A]] | |||
[[Category: Perczel A]] | |||
Latest revision as of 10:20, 9 October 2024
SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGCI[L30R, K31M]SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGCI[L30R, K31M]
Structural highlights
FunctionSGP1_SCHGR In vitro, SGPI-1/SGCI is active against alpha-chymotrypsin and trypsin while SGPI-2/SGTI is active against alpha-chymotrypsin and pancreatic elastase. Publication Abstract from PubMedThe solution structure of three small serine proteinase inhibitors, two natural and one engineered protein, SGCI (Schistocerca gregaria chymotrypsin inhibitor), SGCI[L30R, K31M] and SGTI (Schistocerca gregaria trypsin inhibitor), were determined by homonuclear NMR-spectroscopy. The molecules exhibit different specificities towards target proteinases, where SGCI is a good chymotrypsin inhibitor, its mutant is a potent trypsin inhibitor, and SGTI inhibits both proteinases weakly. Interestingly, SGTI is a much better inhibitor of insect proteinases than of the mammalian ones used in common assays. All three molecules have a similar fold composed from three antiparallel beta-pleated sheets with three disulfide bridges. The proteinase binding loop has a somewhat distinct geometry in all three peptides. Moreover, the stabilization of the structure is different in SGCI and SGTI. Proton-deuterium exchange experiments are indicative of a highly rigid core in SGTI but not in SGCI. We suggest that the observed structural properties play a significant role in the specificity of these inhibitors. Comparative structure analysis of proteinase inhibitors from the desert locust, Schistocerca gregaria.,Gaspari Z, Patthy A, Graf L, Perczel A Eur J Biochem. 2002 Jan;269(2):527-37. PMID:11856311[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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