1kj0: Difference between revisions

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[[Image:1kj0.png|left|200px]]
==SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGTI==
<StructureSection load='1kj0' size='340' side='right' caption='[[1kj0]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1kj0]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KJ0 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kio|1kio]], [[1kgm|1kgm]], [[1pmc|1pmc]]</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=1kj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kj0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kj0 RCSB], [http://www.ebi.ac.uk/pdbsum/1kj0 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.


{{STRUCTURE_1kj0|  PDB=1kj0  |  SCENE=  }}
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>


===SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGTI===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_11856311}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[1kj0]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJ0 OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:011856311</ref><references group="xtra"/>
[[Category: Gaspari, Z.]]
[[Category: Gaspari, Z.]]
[[Category: Graf, L.]]
[[Category: Graf, L.]]

Revision as of 08:42, 8 June 2014

SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGTISOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGTI

Structural highlights

1kj0 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:1kio, 1kgm, 1pmc
Resources:FirstGlance, OCA, RCSB, PDBsum

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Gaspari Z, Patthy A, Graf L, Perczel A. Comparative structure analysis of proteinase inhibitors from the desert locust, Schistocerca gregaria. Eur J Biochem. 2002 Jan;269(2):527-37. PMID:11856311
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