1eag - Revision history

OCA at 10:00, 20 March 2024

OCA — Wed, 20 Mar 2024 10:00:38 GMT

←Older revision		Revision as of 10:00, 20 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1eag]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EAG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1eag]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EAG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A70:N-ETHYL-N-[(4-METHYLPIPERAZIN-1-YL)CARBONYL]-D-PHENYLALANYL-N-[(1S,2S,4R)-4-(BUTYLCARBAMOYL)-1-(CYCLOHEXYLMETHYL)-2-HYDROXY-5-METHYLHEXYL]-L-NORLEUCINAMIDE'>A70</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]] 2.1Å</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] </span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A70:N-ETHYL-N-[(4-METHYLPIPERAZIN-1-YL)CARBONYL]-D-PHENYLALANYL-N-[(1S,2S,4R)-4-(BUTYLCARBAMOYL)-1-(CYCLOHEXYLMETHYL)-2-HYDROXY-5-METHYLHEXYL]-L-NORLEUCINAMIDE'>A70</scene></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=1eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eag OCA], [https://pdbe.org/1eag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eag RCSB], [https://www.ebi.ac.uk/pdbsum/1eag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eag 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=1eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eag OCA], [https://pdbe.org/1eag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eag RCSB], [https://www.ebi.ac.uk/pdbsum/1eag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eag ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/CARP2_CANAX CARP2_CANAX]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=1eag 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=1eag ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	BACKGROUND: Infections caused by Candida albicans, a common fungal pathogen of humans, are increasing in incidence, necessitating development of new therapeutic drugs. Secreted aspartic proteinase (SAP) activity is considered an important virulence factor in these infections and might offer a suitable target for drug design. Amongst the various SAP isozymes, the SAP2 gene product is the major form expressed in a number of C. albicans strains. RESULTS: The three-dimensional structures of SAP2 complexed with the tight-binding inhibitor A70450 (a synthetic hexapeptide analogue) and with the general aspartic proteinase inhibitor pepstatin A (a microbial natural product) have been determined to 2.1 A and 3.0 A resolution, respectively. Although the protein structure retains the main features of a typical aspartic proteinase, it also shows some significant differences, due mainly to several sequence insertions and deletions (as revealed by homology modelling), that alter the shape of the binding cleft. There is also considerable variation in the C-terminal structural domain. CONCLUSIONS: The differences in side chains, and in the conformations adopted by the two inhibitors, particularly at their P4, P3 and P'2 positions (using standard notation for protease-inhibitor residues), allows the A70450 structure to complement, more accurately, that of the substrate-binding site of SAP2. Some differences in the binding clefts of other SAP isoenzymes may be deduced from the SAP2 structure.
-
-	The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors.,Cutfield SM, Dodson EJ, Anderson BF, Moody PC, Marshall CJ, Sullivan PA, Cutfield JF Structure. 1995 Nov 15;3(11):1261-71. PMID:8591036<ref>PMID:8591036</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1eag" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Pepsin\|Pepsin]]		*[[Pepsin\|Pepsin]]
-	*[[Proteinase\|Proteinase]]
	*[[Proteinase 3D structures\|Proteinase 3D structures]]		*[[Proteinase 3D structures\|Proteinase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Candida albicans]]		[[Category: Candida albicans]]
-	[[Category: Candidapepsin]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Cutfield~~, J F~~]]	+	[[Category: Cutfield JF]]
-	[[Category: Cutfield~~, S M]]~~	+	[[Category: Cutfield SM]]
-	~~[[Category: Aspartic protease]]~~	+
-	~~[[Category: Candida albican]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~	+
-	~~[[Category: Sap2~~]]	+

OCA at 09:34, 21 July 2021

OCA — Wed, 21 Jul 2021 09:34:58 GMT

←Older revision		Revision as of 09:34, 21 July 2021
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	<StructureSection load='1eag' size='340' side='right'caption='[[1eag]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1eag' size='340' side='right'caption='[[1eag]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1eag]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1EAG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1eag]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EAG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A70:N-ETHYL-N-[(4-METHYLPIPERAZIN-1-YL)CARBONYL]-D-PHENYLALANYL-N-[(1S,2S,4R)-4-(BUTYLCARBAMOYL)-1-(CYCLOHEXYLMETHYL)-2-HYDROXY-5-METHYLHEXYL]-L-NORLEUCINAMIDE'>A70</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A70:N-ETHYL-N-[(4-METHYLPIPERAZIN-1-YL)CARBONYL]-D-PHENYLALANYL-N-[(1S,2S,4R)-4-(BUTYLCARBAMOYL)-1-(CYCLOHEXYLMETHYL)-2-HYDROXY-5-METHYLHEXYL]-L-NORLEUCINAMIDE'>A70</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] </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=1eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eag OCA], [~~http~~://pdbe.org/1eag PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1eag RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1eag PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1eag 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=1eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eag OCA], [https://pdbe.org/1eag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eag RCSB], [https://www.ebi.ac.uk/pdbsum/1eag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eag ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	*[[Pepsin\|Pepsin]]		*[[Pepsin\|Pepsin]]
	*[[Proteinase\|Proteinase]]		*[[Proteinase\|Proteinase]]
		+	*[[Proteinase 3D structures\|Proteinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:47, 16 October 2019

OCA — Wed, 16 Oct 2019 08:47:15 GMT

←Older revision		Revision as of 08:47, 16 October 2019
Line 1:		Line 1:

	==Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450==		==Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450==
-	<StructureSection load='1eag' size='340' side='right' caption='[[1eag]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='1eag' size='340' side='right'caption='[[1eag]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1eag]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EAG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1eag]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EAG FirstGlance]. <br>
Line 29:		Line 29:

	==See Also==		==See Also==
		+	*[[Pepsin\|Pepsin]]
	*[[Proteinase\|Proteinase]]		*[[Proteinase\|Proteinase]]
	== References ==		== References ==
Line 36:		Line 37:
	[[Category: Candida albicans]]		[[Category: Candida albicans]]
	[[Category: Candidapepsin]]		[[Category: Candidapepsin]]
		+	[[Category: Large Structures]]
	[[Category: Cutfield, J F]]		[[Category: Cutfield, J F]]
	[[Category: Cutfield, S M]]		[[Category: Cutfield, S M]]

OCA at 07:49, 13 December 2017

OCA — Wed, 13 Dec 2017 07:49:36 GMT

←Older revision		Revision as of 07:49, 13 December 2017
Line 1:		Line 1:
		+
	==Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450==		==Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450==
	<StructureSection load='1eag' size='340' side='right' caption='[[1eag]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1eag' size='340' side='right' caption='[[1eag]], [[Resolution\|resolution]] 2.10Å' scene=''>
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A70:N-ETHYL-N-[(4-METHYLPIPERAZIN-1-YL)CARBONYL]-D-PHENYLALANYL-N-[(1S,2S,4R)-4-(BUTYLCARBAMOYL)-1-(CYCLOHEXYLMETHYL)-2-HYDROXY-5-METHYLHEXYL]-L-NORLEUCINAMIDE'>A70</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A70:N-ETHYL-N-[(4-METHYLPIPERAZIN-1-YL)CARBONYL]-D-PHENYLALANYL-N-[(1S,2S,4R)-4-(BUTYLCARBAMOYL)-1-(CYCLOHEXYLMETHYL)-2-HYDROXY-5-METHYLHEXYL]-L-NORLEUCINAMIDE'>A70</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] </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=1eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eag OCA], [http://pdbe.org/1eag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eag RCSB], [http://www.ebi.ac.uk/pdbsum/1eag 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=1eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eag OCA], [http://pdbe.org/1eag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eag RCSB], [http://www.ebi.ac.uk/pdbsum/1eag PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1eag ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ea/1eag_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ea/1eag_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>
Line 28:		Line 29:

	==See Also==		==See Also==
-	*[[Pepsin\|Pepsin]]
	*[[Proteinase\|Proteinase]]		*[[Proteinase\|Proteinase]]
	== References ==		== References ==

OCA at 05:33, 9 February 2016

OCA — Tue, 09 Feb 2016 05:33:02 GMT

←Older revision		Revision as of 05:33, 9 February 2016
Line 15:		Line 15:
	<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=1eag ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 19:07, 10 September 2015

OCA — Thu, 10 Sep 2015 19:07:20 GMT

←Older revision		Revision as of 19:07, 10 September 2015
Line 5:		Line 5:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A70:N-ETHYL-N-[(4-METHYLPIPERAZIN-1-YL)CARBONYL]-D-PHENYLALANYL-N-[(1S,2S,4R)-4-(BUTYLCARBAMOYL)-1-(CYCLOHEXYLMETHYL)-2-HYDROXY-5-METHYLHEXYL]-L-NORLEUCINAMIDE'>A70</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A70:N-ETHYL-N-[(4-METHYLPIPERAZIN-1-YL)CARBONYL]-D-PHENYLALANYL-N-[(1S,2S,4R)-4-(BUTYLCARBAMOYL)-1-(CYCLOHEXYLMETHYL)-2-HYDROXY-5-METHYLHEXYL]-L-NORLEUCINAMIDE'>A70</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] </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=1eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eag OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eag RCSB], [http://www.ebi.ac.uk/pdbsum/1eag 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=1eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eag OCA], [http://pdbe.org/1eag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eag RCSB], [http://www.ebi.ac.uk/pdbsum/1eag PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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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 1eag" style="background-color:#fffaf0;"></div>

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

OCA at 21:47, 22 December 2014

OCA — Mon, 22 Dec 2014 21:47:09 GMT

←Older revision		Revision as of 21:47, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1eag]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EAG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1eag]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EAG FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A70:N-ETHYL-N-[(4-METHYLPIPERAZIN-1-YL)CARBONYL]-D-PHENYLALANYL-N-[(1S,2S,4R)-4-(BUTYLCARBAMOYL)-1-(CYCLOHEXYLMETHYL)-2-HYDROXY-5-METHYLHEXYL]-L-NORLEUCINAMIDE'>A70</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A70:N-ETHYL-N-[(4-METHYLPIPERAZIN-1-YL)CARBONYL]-D-PHENYLALANYL-N-[(1S,2S,4R)-4-(BUTYLCARBAMOYL)-1-(CYCLOHEXYLMETHYL)-2-HYDROXY-5-METHYLHEXYL]-L-NORLEUCINAMIDE'>A70</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eag OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eag RCSB], [http://www.ebi.ac.uk/pdbsum/1eag 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=1eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eag OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eag RCSB], [http://www.ebi.ac.uk/pdbsum/1eag PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:
	[[Category: Candida albicans]]		[[Category: Candida albicans]]
	[[Category: Candidapepsin]]		[[Category: Candidapepsin]]
-	[[Category: Cutfield, J F.]]	+	[[Category: Cutfield, J F]]
-	[[Category: Cutfield, S M.]]	+	[[Category: Cutfield, S M]]
	[[Category: Aspartic protease]]		[[Category: Aspartic protease]]
	[[Category: Candida albican]]		[[Category: Candida albican]]
	[[Category: Hydrolase-hydrolase inhibitor complex]]		[[Category: Hydrolase-hydrolase inhibitor complex]]
	[[Category: Sap2]]		[[Category: Sap2]]

OCA at 10:37, 10 September 2014

OCA — Wed, 10 Sep 2014 10:37:42 GMT

←Older revision		Revision as of 10:37, 10 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1eag.~~png\|left~~\|200px]]	+	==Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450==
		+	<StructureSection load='1eag' size='340' side='right' caption='[[1eag]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1eag]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EAG FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A70:N-ETHYL-N-[(4-METHYLPIPERAZIN-1-YL)CARBONYL]-D-PHENYLALANYL-N-[(1S,2S,4R)-4-(BUTYLCARBAMOYL)-1-(CYCLOHEXYLMETHYL)-2-HYDROXY-5-METHYLHEXYL]-L-NORLEUCINAMIDE'>A70</scene><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eag OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eag RCSB], [http://www.ebi.ac.uk/pdbsum/1eag PDBsum]</span></td></tr>
		+	<table>
		+	== 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/ea/1eag_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 ==
		+	BACKGROUND: Infections caused by Candida albicans, a common fungal pathogen of humans, are increasing in incidence, necessitating development of new therapeutic drugs. Secreted aspartic proteinase (SAP) activity is considered an important virulence factor in these infections and might offer a suitable target for drug design. Amongst the various SAP isozymes, the SAP2 gene product is the major form expressed in a number of C. albicans strains. RESULTS: The three-dimensional structures of SAP2 complexed with the tight-binding inhibitor A70450 (a synthetic hexapeptide analogue) and with the general aspartic proteinase inhibitor pepstatin A (a microbial natural product) have been determined to 2.1 A and 3.0 A resolution, respectively. Although the protein structure retains the main features of a typical aspartic proteinase, it also shows some significant differences, due mainly to several sequence insertions and deletions (as revealed by homology modelling), that alter the shape of the binding cleft. There is also considerable variation in the C-terminal structural domain. CONCLUSIONS: The differences in side chains, and in the conformations adopted by the two inhibitors, particularly at their P4, P3 and P'2 positions (using standard notation for protease-inhibitor residues), allows the A70450 structure to complement, more accurately, that of the substrate-binding site of SAP2. Some differences in the binding clefts of other SAP isoenzymes may be deduced from the SAP2 structure.

-	~~{{STRUCTURE_1eag\| PDB=1eag \| SCENE= }}~~	+	The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors.,Cutfield SM, Dodson EJ, Anderson BF, Moody PC, Marshall CJ, Sullivan PA, Cutfield JF Structure. 1995 Nov 15;3(11):1261-71. PMID:8591036<ref>PMID:8591036</ref>

-	~~===Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[1eag]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Candida_albicans Candida albicans]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1EAG OCA].~~	+

	==See Also==		==See Also==
	*[[Pepsin\|Pepsin]]		*[[Pepsin\|Pepsin]]
-		+	*[[Proteinase\|Proteinase]]
-	==~~Reference~~==	+	== References ==
-	<~~ref group="xtra">PMID:008591036<~~/~~ref~~><~~references group="xtra"~~/>	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Candida albicans]]		[[Category: Candida albicans]]
	[[Category: Candidapepsin]]		[[Category: Candidapepsin]]

OCA at 14:07, 8 November 2012

OCA — Thu, 08 Nov 2012 14:07:44 GMT

←Older revision		Revision as of 14:07, 8 November 2012
Line 5:		Line 5:
	===Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450===		===Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450===

-	{{ABSTRACT_PUBMED_8591036}}

	==About this Structure==		==About this Structure==

OCA at 12:48, 20 October 2012

OCA — Sat, 20 Oct 2012 12:48:37 GMT

←Older revision		Revision as of 12:48, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1eag]] is a 1 chain structure ~~of [[Pepsin]]~~ with sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAG OCA].	+	[[1eag]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAG OCA].

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