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New page: left|200px<br /><applet load="1kj0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kj0" /> '''SOLUTION STRUCTURE OF THE SMALL SERINE PROTE...
 
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[[Image:1kj0.jpg|left|200px]]<br /><applet load="1kj0" size="450" color="white" frame="true" align="right" spinBox="true"  
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caption="1kj0" />
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'''SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGTI'''<br />
'''SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGTI'''<br />


==Overview==
==Overview==
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.


==About this Structure==
==About this Structure==
1KJ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KJ0 OCA].  
1KJ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJ0 OCA].  


==Reference==
==Reference==
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[[Category: serine protease inhibition]]
[[Category: serine protease inhibition]]


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Revision as of 14:34, 21 February 2008

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1kj0

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SOLUTION STRUCTURE OF THE SMALL SERINE PROTEASE INHIBITOR SGTI

OverviewOverview

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.

About this StructureAbout this Structure

1KJ0 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

ReferenceReference

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

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