1kio: Difference between revisions
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==SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGCI[L30R, K31M]== | ==SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGCI[L30R, K31M]== | ||
<StructureSection load='1kio' size='340' side='right' caption='[[1kio]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='1kio' size='340' side='right'caption='[[1kio]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1kio]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KIO FirstGlance]. <br> | <table><tr><td colspan='2'>[[1kio]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KIO FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1kio" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1kio" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Chymotrypsin inhibitor 3D structures|Chymotrypsin inhibitor 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Gaspari, Z]] | [[Category: Gaspari, Z]] | ||
[[Category: Graf, L]] | [[Category: Graf, L]] | ||
Revision as of 16:07, 17 July 2019
SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGCI[L30R, K31M]SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGCI[L30R, K31M]
Structural highlights
Function[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. 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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