1ppg: Difference between revisions

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New page: left|200px<br /> <applet load="1ppg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ppg, resolution 2.3Å" /> '''THE REFINED 2.3 ANGS...
 
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[[Image:1ppg.gif|left|200px]]<br />
[[Image:1ppg.gif|left|200px]]<br /><applet load="1ppg" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1ppg" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1ppg, resolution 2.3&Aring;" />
caption="1ppg, resolution 2.3&Aring;" />
'''THE REFINED 2.3 ANGSTROMS CRYSTAL STRUCTURE OF HUMAN LEUKOCYTE ELASTASE IN A COMPLEX WITH A VALINE CHLOROMETHYL KETONE INHIBITOR'''<br />
'''THE REFINED 2.3 ANGSTROMS CRYSTAL STRUCTURE OF HUMAN LEUKOCYTE ELASTASE IN A COMPLEX WITH A VALINE CHLOROMETHYL KETONE INHIBITOR'''<br />


==Overview==
==Overview==
The stoichiometric complex formed between human leukocyte elastase and a, synthetic MeO-Suc-Ala-Ala-Pro-Val chloromethyl ketone inhibitor was, co-crystallized and its X-ray structure determined, using Patterson search, methods. Its structure has been crystallographically refined to a final R, value of 0.145 (8.0 and 2.3 A). The enzyme structure is very similar to, that recently observed in a complex formed with the ovomucoid third domain, from turkey [(1986) EMBO J. 5,2453-2458]. The rms deviation of all, alpha-carbon atoms is 0.32 A. The peptidic inhibitor is bound in a similar, overall conformation as the ovomucoid binding segment. Covalent bonds are, formed between Val-P1 of the inhibitor and His-57 NE2 and Ser-195 OG of, the enzyme. The carbonyl carbon is tetrahedrally deformed to a hemiketal., The valine side chain is arranged in the S1 pocket in the g-conformation.
The stoichiometric complex formed between human leukocyte elastase and a synthetic MeO-Suc-Ala-Ala-Pro-Val chloromethyl ketone inhibitor was co-crystallized and its X-ray structure determined, using Patterson search methods. Its structure has been crystallographically refined to a final R value of 0.145 (8.0 and 2.3 A). The enzyme structure is very similar to that recently observed in a complex formed with the ovomucoid third domain from turkey [(1986) EMBO J. 5,2453-2458]. The rms deviation of all alpha-carbon atoms is 0.32 A. The peptidic inhibitor is bound in a similar overall conformation as the ovomucoid binding segment. Covalent bonds are formed between Val-P1 of the inhibitor and His-57 NE2 and Ser-195 OG of the enzyme. The carbonyl carbon is tetrahedrally deformed to a hemiketal. The valine side chain is arranged in the S1 pocket in the g-conformation.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1PPG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Active as [http://en.wikipedia.org/wiki/Leukocyte_elastase Leukocyte elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.37 3.4.21.37] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PPG OCA].  
1PPG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Active as [http://en.wikipedia.org/wiki/Leukocyte_elastase Leukocyte elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.37 3.4.21.37] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PPG OCA].  


==Reference==
==Reference==
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[[Category: hydrolase(serine proteinase)]]
[[Category: hydrolase(serine proteinase)]]


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