3h7d - Revision history

OCA at 07:17, 6 September 2023

2023-09-06T07:17:22Z

←Older revision		Revision as of 07:17, 6 September 2023
Line 3:		Line 3:
	<StructureSection load='3h7d' size='340' side='right'caption='[[3h7d]], [[Resolution\|resolution]] 2.24Å' scene=''>		<StructureSection load='3h7d' size='340' side='right'caption='[[3h7d]], [[Resolution\|resolution]] 2.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3h7d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H7D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3h7d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H7D FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~"><~~scene name='pdbligand=CA:CALCIUM+ION'~~>CA</~~scene~~>, <~~scene name~~='~~pdbligand~~=~~E64:N-~~[N-[~~1-HYDROXYCARBOXYETHYL-CARBONYL~~]~~LEUCYLAMINO-BUTYL~~]~~-GUANIDINE'~~>~~E64~~</~~scene~~>, <scene name='pdbligand=ASG:2-DEOXY-2-ACETAMIDO-BETA-D-GALACTOSE-4-SULFATE'>ASG</scene>, <scene name='pdbligand=BDP:BETA-D-GLUCOPYRANURONIC+ACID'>BDP</scene><~~/td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.242Å</td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b~~></td><~~td class~~=~~"sblockDat"><div style~~=~~'overflow~~: ~~auto; max~~-~~height: 3em;'>~~[[~~3c9e\|3c9e~~]]~~</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASG:2-DEOXY-2-ACETAMIDO-BETA-D-GALACTOSE-4-SULFATE'>ASG</scene>, <scene name='pdbligand=BDP:BETA-D-GLUCOPYRANURONIC+ACID'>BDP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene></td></tr>
-	~~<tr id='gene~~'>~~<td class="sblockLbl"><b>[[Gene\|Gene:]]~~</~~b></td><td class="sblockDat">CTSK, CTSO, CTSO2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cathepsin_K Cathepsin K], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.38 3.4.22.38] </span></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3h7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h7d OCA], [https://pdbe.org/3h7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h7d RCSB], [https://www.ebi.ac.uk/pdbsum/3h7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h7d ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3h7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h7d OCA], [https://pdbe.org/3h7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h7d RCSB], [https://www.ebi.ac.uk/pdbsum/3h7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h7d ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:[https://omim.org/entry/265800 265800]]. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature.<ref>PMID:8703060</ref> <ref>PMID:9529353</ref> <ref>PMID:10491211</ref> <ref>PMID:10878663</ref>	+	[https://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:[https://omim.org/entry/265800 265800]. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature.<ref>PMID:8703060</ref> <ref>PMID:9529353</ref> <ref>PMID:10491211</ref> <ref>PMID:10878663</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation.	+	[https://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN] Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 40:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Cathepsin K]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bromme, D]]	+	[[Category: Bromme D]]
-	[[Category: Cherney~~, M M~~]]	+	[[Category: Cherney MM]]
-	[[Category: James~~, M N.G~~]]	+	[[Category: James MNG]]
-	[[Category: Kienetz, M]]	+	[[Category: Kienetz M]]
-	~~[[Category: Cathepsin k mutant]]~~	+
-	~~[[Category: Disease mutation]]~~	+
-	~~[[Category: Disulfide bond]]~~	+
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Glycosaminoglycan]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Lysosome]]~~	+
-	~~[[Category: Protease]]~~	+
-	~~[[Category: Sulfhydryl peptidase]]~~	+
-	~~[[Category: Ternary complex]]~~	+
-	~~[[Category: Thiol protease]]~~	+
-	~~[[Category: Zymogen~~]]	+

OCA at 11:55, 13 October 2021

2021-10-13T11:55:42Z

OCA at 08:17, 24 July 2019

2019-07-24T08:17:20Z

←Older revision		Revision as of 08:17, 24 July 2019
Line 1:		Line 1:

	==The crystal structure of the cathepsin K Variant M5 in complex with chondroitin-4-sulfate==		==The crystal structure of the cathepsin K Variant M5 in complex with chondroitin-4-sulfate==
-	<StructureSection load='3h7d' size='340' side='right' caption='[[3h7d]], [[Resolution\|resolution]] 2.24Å' scene=''>	+	<StructureSection load='3h7d' size='340' side='right'caption='[[3h7d]], [[Resolution\|resolution]] 2.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3h7d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H7D FirstGlance]. <br>		<table><tr><td colspan='2'>[[3h7d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H7D FirstGlance]. <br>
Line 35:		Line 35:

	==See Also==		==See Also==
-	*[[Cathepsin\|Cathepsin]]	+	*[[Cathepsin 3D structures\|Cathepsin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 42:		Line 42:
	[[Category: Cathepsin K]]		[[Category: Cathepsin K]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Bromme, D]]		[[Category: Bromme, D]]
	[[Category: Cherney, M M]]		[[Category: Cherney, M M]]

OCA at 05:22, 7 December 2018

2018-12-07T05:22:28Z

←Older revision		Revision as of 05:22, 7 December 2018
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3h7d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H7D FirstGlance]. <br>		<table><tr><td colspan='2'>[[3h7d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H7D FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:~~CALCIUM+ION~~'>CA</scene>, <scene name='pdbligand=~~E64~~:N-[N-~~[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE~~'>~~E64~~</scene>, <scene name='pdbligand=~~ASG~~:~~2-DEOXY-2-ACETAMIDO-BETA-D-GALACTOSE-4-SULFATE~~'>~~ASG~~</scene>, <scene name='pdbligand=~~BDP~~:~~BETA~~-D-~~GLUCOPYRANURONIC+ACID~~'>~~BDP~~</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASG:2-DEOXY-2-ACETAMIDO-BETA-D-GALACTOSE-4-SULFATE'>ASG</scene>, <scene name='pdbligand=BDP:BETA-D-GLUCOPYRANURONIC+ACID'>BDP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3c9e\|3c9e]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3c9e\|3c9e]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CTSK, CTSO, CTSO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CTSK, CTSO, CTSO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
Line 18:		Line 18:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h7/3h7d_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h7/3h7d_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 21:15, 5 August 2016

2016-08-05T21:15:51Z

←Older revision		Revision as of 21:15, 5 August 2016
Line 1:		Line 1:
		+
	==The crystal structure of the cathepsin K Variant M5 in complex with chondroitin-4-sulfate==		==The crystal structure of the cathepsin K Variant M5 in complex with chondroitin-4-sulfate==
	<StructureSection load='3h7d' size='340' side='right' caption='[[3h7d]], [[Resolution\|resolution]] 2.24Å' scene=''>		<StructureSection load='3h7d' size='340' side='right' caption='[[3h7d]], [[Resolution\|resolution]] 2.24Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CTSK, CTSO, CTSO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CTSK, CTSO, CTSO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_K Cathepsin K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.38 3.4.22.38] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_K Cathepsin K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.38 3.4.22.38] </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=3h7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h7d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h7d RCSB], [http://www.ebi.ac.uk/pdbsum/3h7d 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=3h7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h7d OCA], [http://pdbe.org/3h7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h7d RCSB], [http://www.ebi.ac.uk/pdbsum/3h7d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3h7d ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 21:		Line 22:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3h7d ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 31:		Line 32:
	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 3h7d" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 16:33, 21 December 2014

2014-12-21T16:33:54Z

←Older revision		Revision as of 16:33, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3h7d\| PDB=3h7d \| SCENE= }}~~	+	==The crystal structure of the cathepsin K Variant M5 in complex with chondroitin-4-sulfate==
-	===The crystal structure of the cathepsin K Variant M5 in complex with chondroitin-4-sulfate===	+	<StructureSection load='3h7d' size='340' side='right' caption='[[3h7d]], [[Resolution\|resolution]] 2.24Å' scene=''>
-	~~{{ABSTRACT_PUBMED_21193413}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3h7d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H7D FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <scene name='pdbligand=ASG:2-DEOXY-2-ACETAMIDO-BETA-D-GALACTOSE-4-SULFATE'>ASG</scene>, <scene name='pdbligand=BDP:BETA-D-GLUCOPYRANURONIC+ACID'>BDP</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3c9e\|3c9e]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CTSK, CTSO, CTSO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_K Cathepsin K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.38 3.4.22.38] </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=3h7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h7d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h7d RCSB], [http://www.ebi.ac.uk/pdbsum/3h7d PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:[http://omim.org/entry/265800 265800]]. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature.<ref>PMID:8703060</ref> <ref>PMID:9529353</ref> <ref>PMID:10491211</ref> <ref>PMID:10878663</ref>		[[http://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:[http://omim.org/entry/265800 265800]]. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature.<ref>PMID:8703060</ref> <ref>PMID:9529353</ref> <ref>PMID:10491211</ref> <ref>PMID:10878663</ref>
-		+	== Function ==
-	==Function==	+
	[[http://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation.		[[http://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation.
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h7/3h7d_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	In the presence of oligomeric chondroitin 4-sulfate (C4-S), cathepsin K (catK) forms a specific complex that was shown to be the source of the major collagenolytic activity in bone osteoclasts. C4-S forms multiple contacts with amino acid residues on the backside of the catK molecule that help to facilitate complex formation. As cathepsin L does not exhibit a significant collagenase activity in the presence or in the absence of C4-S, we substituted the C4-S interacting residues in catK with those of cathepsin L. Variants revealed altered collagenolytic activities with the largest inhibitory effect shown by the hexavariant M5. None of the variants showed a reduction in their gelatinolytic and peptidolytic activities when compared with wild-type catK, indicating no structural alteration within their active sites. However, the crystal structure of the M5 variant in the presence of oligomeric C4-S revealed a different binding of chondroitin 4-sulfate. C4-S is not continuously ordered as it is in the wild-type catK.C4-S complex. The orientation and the direction of the hexasaccharide on the catK surface have changed, so that the hexasaccharide is positioned between two symmetry-related molecules. Only one M5 variant molecule of the dimer that is present in the asymmetric unit interacts with C4-S. These substitutions have changed the mode of catK binding to C4-S and, as a result, have likely affected the collagenolytic potential of the variant. The data presented here support our hypothesis that distinct catK/C4-S interactions are necessary for the collagenolytic activity of the enzyme.

-	~~==About this~~ Structure==	+	Structure-activity analysis of cathepsin K/chondroitin 4-sulfate interactions.,Cherney MM, Lecaille F, Kienitz M, Nallaseth FS, Li Z, James MN, Bromme D J Biol Chem. 2011 Mar 18;286(11):8988-98. Epub 2010 Dec 30. PMID:21193413<ref>PMID:21193413</ref>
-	~~[[3h7d]] is a 2 chain structure with sequence from [http:/~~/en.~~wikipedia~~.~~org/wiki/Human Human]~~. ~~Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=3H7D OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Cathepsin\|Cathepsin]]		*[[Cathepsin\|Cathepsin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:021193413</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Cathepsin K]]		[[Category: Cathepsin K]]
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Bromme, D.]]	+	[[Category: Bromme, D]]
-	[[Category: Cherney, M M.]]	+	[[Category: Cherney, M M]]
-	[[Category: James, M N.G.]]	+	[[Category: James, M N.G]]
-	[[Category: Kienetz, M.]]	+	[[Category: Kienetz, M]]
	[[Category: Cathepsin k mutant]]		[[Category: Cathepsin k mutant]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]

OCA at 06:59, 15 January 2014

2014-01-15T06:59:01Z

←Older revision		Revision as of 06:59, 15 January 2014
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	{{STRUCTURE_3h7d\| PDB=3h7d \| SCENE= }}		{{STRUCTURE_3h7d\| PDB=3h7d \| SCENE= }}
	===The crystal structure of the cathepsin K Variant M5 in complex with chondroitin-4-sulfate===		===The crystal structure of the cathepsin K Variant M5 in complex with chondroitin-4-sulfate===
-	{{~~ABSTRACT_PUBMED_021193413~~}}	+	{{ABSTRACT_PUBMED_21193413}}

	==Disease==		==Disease==
-	[[http://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:[http://omim.org/entry/265800 265800]]. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature.<ref>PMID:8703060</ref><ref>PMID:9529353</ref><ref>PMID:10491211</ref><ref>PMID:10878663</ref>	+	[[http://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:[http://omim.org/entry/265800 265800]]. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature.<ref>PMID:8703060</ref> <ref>PMID:9529353</ref> <ref>PMID:10491211</ref> <ref>PMID:10878663</ref>

	==Function==		==Function==
Line 10:		Line 10:

	==About this Structure==		==About this Structure==
-	[[3h7d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H7D OCA].	+	[[3h7d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H7D OCA].

	==See Also==		==See Also==
Line 18:		Line 18:
	<ref group="xtra">PMID:021193413</ref><references group="xtra"/><references/>		<ref group="xtra">PMID:021193413</ref><references group="xtra"/><references/>
	[[Category: Cathepsin K]]		[[Category: Cathepsin K]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Bromme, D.]]		[[Category: Bromme, D.]]
	[[Category: Cherney, M M.]]		[[Category: Cherney, M M.]]

OCA at 05:32, 25 March 2013

2013-03-25T05:32:18Z

←Older revision		Revision as of 05:32, 25 March 2013
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-	[[Image:3h7d.png\|left\|200px]]
-
	{{STRUCTURE_3h7d\| PDB=3h7d \| SCENE= }}		{{STRUCTURE_3h7d\| PDB=3h7d \| SCENE= }}
-
	===The crystal structure of the cathepsin K Variant M5 in complex with chondroitin-4-sulfate===		===The crystal structure of the cathepsin K Variant M5 in complex with chondroitin-4-sulfate===
		+	{{ABSTRACT_PUBMED_021193413}}

-	~~{{ABSTRACT_PUBMED_021193413}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:[http://omim.org/entry/265800 265800]]. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature.<ref>PMID:8703060</ref><ref>PMID:9529353</ref><ref>PMID:10491211</ref><ref>PMID:10878663</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation.

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:021193413</ref><references group="xtra"/>	+	<ref group="xtra">PMID:021193413</ref><references group="xtra"/><references/>
	[[Category: Cathepsin K]]		[[Category: Cathepsin K]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 13:23, 20 October 2012

2012-10-20T13:23:16Z

←Older revision		Revision as of 13:23, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3h7d]] is a 2 chain structure ~~of [[Cathepsin]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H7D OCA].	+	[[3h7d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H7D OCA].

	==See Also==		==See Also==

OCA at 11:48, 26 July 2012

2012-07-26T11:48:14Z

←Older revision		Revision as of 11:48, 26 July 2012
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	[[Image:3h7d.png\|left\|200px]]		[[Image:3h7d.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3h7d", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
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	{{STRUCTURE_3h7d\| PDB=3h7d \| SCENE= }}		{{STRUCTURE_3h7d\| PDB=3h7d \| SCENE= }}

	===The crystal structure of the cathepsin K Variant M5 in complex with chondroitin-4-sulfate===		===The crystal structure of the cathepsin K Variant M5 in complex with chondroitin-4-sulfate===

		+	{{ABSTRACT_PUBMED_021193413}}

	==About this Structure==		==About this Structure==
Line 16:		Line 11:

	==See Also==		==See Also==
-	*[[Cathepsin]]	+	*[[Cathepsin\|Cathepsin]]
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021193413</ref><references group="xtra"/>
	[[Category: Cathepsin K]]		[[Category: Cathepsin K]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

←Older revision		Revision as of 11:55, 13 October 2021
Line 3:		Line 3:
	<StructureSection load='3h7d' size='340' side='right'caption='[[3h7d]], [[Resolution\|resolution]] 2.24Å' scene=''>		<StructureSection load='3h7d' size='340' side='right'caption='[[3h7d]], [[Resolution\|resolution]] 2.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3h7d]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H7D OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3H7D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3h7d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H7D FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~ASG~~:~~2-DEOXY-2-ACETAMIDO-BETA-D-GALACTOSE-4-SULFATE~~'>~~ASG~~</scene>, <scene name='pdbligand=~~BDP~~:~~BETA~~-D-~~GLUCOPYRANURONIC+ACID~~'>~~BDP~~</scene>, <scene name='pdbligand=CA:~~CALCIUM+ION~~'>CA</scene>, <scene name='pdbligand=~~E64~~:N-[N-~~[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE~~'>~~E64~~</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <scene name='pdbligand=ASG:2-DEOXY-2-ACETAMIDO-BETA-D-GALACTOSE-4-SULFATE'>ASG</scene>, <scene name='pdbligand=BDP:BETA-D-GLUCOPYRANURONIC+ACID'>BDP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3c9e\|3c9e]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3c9e\|3c9e]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CTSK, CTSO, CTSO2 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CTSK, CTSO, CTSO2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Cathepsin_K Cathepsin K], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.38 3.4.22.38] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cathepsin_K Cathepsin K], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.38 3.4.22.38] </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=3h7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h7d OCA], [~~http~~://pdbe.org/3h7d PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3h7d RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3h7d PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3h7d ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3h7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h7d OCA], [https://pdbe.org/3h7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h7d RCSB], [https://www.ebi.ac.uk/pdbsum/3h7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h7d ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:[~~http~~://omim.org/entry/265800 265800]]. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature.<ref>PMID:8703060</ref> <ref>PMID:9529353</ref> <ref>PMID:10491211</ref> <ref>PMID:10878663</ref>	+	[[https://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:[https://omim.org/entry/265800 265800]]. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature.<ref>PMID:8703060</ref> <ref>PMID:9529353</ref> <ref>PMID:10491211</ref> <ref>PMID:10878663</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation.	+	[[https://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]