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4tkx
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Structure of Protease== |
| + | <StructureSection load='4tkx' size='340' side='right' caption='[[4tkx]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4tkx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TKX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TKX FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TCK:N-[(1S)-5-AMINO-1-(CHLOROACETYL)PENTYL]-4-METHYLBENZENESULFONAMIDE'>TCK</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Gingipain_K Gingipain K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.47 3.4.22.47] </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=4tkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tkx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tkx RCSB], [http://www.ebi.ac.uk/pdbsum/4tkx PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/KGP83_PORGN KGP83_PORGN]] Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria (By similarity).[UniProtKB:B2RLK2] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The oral pathogen Porphyromonas gingivalis is a keystone pathogen in the development of chronic periodontitis. Gingipains, the principle virulence factors of P. gingivalis are multidomain, cell-surface proteins containing a cysteine protease domain. The lysine specific gingipain, Kgp, is a critical virulence factor of P. gingivalis. We have determined the X-ray crystal structure of the lysine-specific protease domain of Kgp to 1.6 A resolution. The structure provides insights into the mechanism of substrate specificity and catalysis. | ||
| - | + | Structure of the lysine specific protease Kgp from Porphyromonas gingivalis, a target for improved oral health.,Gorman MA, Seers CA, Michell BJ, Feil SC, Huq NL, Cross KJ, Reynolds EC, Parker MW Protein Sci. 2015 Jan;24(1):162-6. doi: 10.1002/pro.2589. Epub 2014 Dec 3. PMID:25327141<ref>PMID:25327141</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Gingipain K]] | ||
| + | [[Category: Gorman, M A]] | ||
| + | [[Category: Parker, M W]] | ||
| + | [[Category: Co-valent inhibitor]] | ||
| + | [[Category: Cysteine protease]] | ||
| + | [[Category: Gingivali]] | ||
| + | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
| + | [[Category: Kgp]] | ||
Revision as of 14:48, 31 December 2014
Structure of Protease
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