1k9o: Difference between revisions
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<StructureSection load='1k9o' size='340' side='right' caption='[[1k9o]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1k9o' size='340' side='right' caption='[[1k9o]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1k9o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1k9o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Carolina_sphinx Carolina sphinx]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1i99 1i99]. The May 2004 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Serpins'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2004_5 10.2210/rcsb_pdb/mom_2004_5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K9O FirstGlance]. <br> | ||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></td></tr> | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k9o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1k9o RCSB], [http://www.ebi.ac.uk/pdbsum/1k9o PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k9o OCA], [http://pdbe.org/1k9o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k9o RCSB], [http://www.ebi.ac.uk/pdbsum/1k9o PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1k9o" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Buffalo rat]] | ||
[[Category: Carolina sphinx]] | |||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: Serpins]] | [[Category: Serpins]] | ||
[[Category: Trypsin]] | [[Category: Trypsin]] | ||
Revision as of 15:32, 10 September 2015
CRYSTAL STRUCTURE OF MICHAELIS SERPIN-TRYPSIN COMPLEXCRYSTAL STRUCTURE OF MICHAELIS SERPIN-TRYPSIN COMPLEX
Structural highlights
Function[SERA_MANSE] Inhibits elastase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSerine protease inhibitors (serpins) regulate the activities of circulating proteases. Serpins inhibit proteases by acylating the serine hydroxyl at their active sites. Before deacylation and complete proteolysis of the serpin can occur, massive conformational changes are triggered in the serpin while maintaining the covalent linkage between the protease and serpin. Here we report the structure of a serpin-trypsin Michaelis complex, which we visualized by using the S195A trypsin mutant to prevent covalent complex formation. This encounter complex reveals a more extensive interaction surface than that present in small inhibitor-protease complexes and is a template for modeling other serpin-protease pairs. Mutations of several serpin residues at the interface reduced the inhibitory activity of the serpin. The serine residue C-terminal to the scissile peptide bond is found in a closer than usual interaction with His 57 at the active site of trypsin. The structure of a Michaelis serpin-protease complex.,Ye S, Cech AL, Belmares R, Bergstrom RC, Tong Y, Corey DR, Kanost MR, Goldsmith EJ Nat Struct Biol. 2001 Nov;8(11):979-83. PMID:11685246[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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