1kj0: Difference between revisions

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"  
[[Image:1kj0.jpg|left|200px]]<br /><applet load="1kj0" size="350" color="white" frame="true" align="right" spinBox="true"  
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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