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[[ | ==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=''> | |||
== 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> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kgm|1kgm]], [[1pmc|1pmc]], [[1kj0|1kj0]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kio OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kio RCSB], [http://www.ebi.ac.uk/pdbsum/1kio PDBsum]</span></td></tr> | |||
<table> | |||
<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. | |||
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> | |||
==See Also== | ==See Also== | ||
*[[Chymotrypsin Inhibitor|Chymotrypsin Inhibitor]] | *[[Chymotrypsin Inhibitor|Chymotrypsin Inhibitor]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Gaspari, Z.]] | [[Category: Gaspari, Z.]] | ||
[[Category: Graf, L.]] | [[Category: Graf, L.]] | ||
Revision as of 14:47, 28 September 2014
SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGCI[L30R, K31M]SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGCI[L30R, K31M]
Structural highlights
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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