4cdc - Revision history

OCA at 12:08, 20 December 2023

2023-12-20T12:08:11Z

← Older revision		Revision as of 12:08, 20 December 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cdc]] is a 12 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=4CDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CDC FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cdc]] is a 12 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=4CDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CDC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6AO:(2S)-2-AZANYL-N-[(2S)-1-AZANYLIDENE-3-(4-PHENYLPHENYL)PROPAN-2-YL]BUTANAMIDE'>6AO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.4Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6AO:(2S)-2-AZANYL-N-[(2S)-1-AZANYLIDENE-3-(4-PHENYLPHENYL)PROPAN-2-YL]BUTANAMIDE'>6AO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4cdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cdc OCA], [https://pdbe.org/4cdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cdc RCSB], [https://www.ebi.ac.uk/pdbsum/4cdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cdc 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=4cdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cdc OCA], [https://pdbe.org/4cdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cdc RCSB], [https://www.ebi.ac.uk/pdbsum/4cdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cdc ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[https://www.uniprot.org/uniprot/CATC_HUMAN CATC_HUMAN]] Defects in CTSC are a cause of Papillon-Lefevre syndrome (PLS) [MIM:[https://omim.org/entry/245000 245000]]; also known as keratosis palmoplantaris with periodontopathia. PLS is an autosomal recessive disorder characterized by palmoplantar keratosis and severe periodontitis affecting deciduous and permanent dentitions and resulting in premature tooth loss. The palmoplantar keratotic phenotype vary from mild psoriasiform scaly skin to overt hyperkeratosis. Keratosis also affects other sites such as elbows and knees.<ref>PMID:11180601</ref> <ref>PMID:12809647</ref> <ref>PMID:10581027</ref> <ref>PMID:10662808</ref> <ref>PMID:11106356</ref> <ref>PMID:11180012</ref> <ref>PMID:11886537</ref> <ref>PMID:11158173</ref> <ref>PMID:12112662</ref> <ref>PMID:14974080</ref> <ref>PMID:15108292</ref> <ref>PMID:15991336</ref> Defects in CTSC are a cause of Haim-Munk syndrome (HMS) [MIM:[https://omim.org/entry/245010 245010]]; also known as keratosis palmoplantaris with periodontopathia and onychogryposis or Cochin Jewish disorder. HMS is an autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis.<ref>PMID:10662807</ref> Defects in CTSC are a cause of aggressive periodontititis type 1 (AP1) [MIM:[https://omim.org/entry/170650 170650]]; also known as juvenile periodontitis (JPD) and prepubertal periodontitis (PPP). AP1 is characterized by severe and protracted gingival infections, leading to tooth loss. AP1 inheritance is autosomal dominant.<ref>PMID:10662808</ref> <ref>PMID:14974080</ref>		[https://www.uniprot.org/uniprot/CATC_HUMAN CATC_HUMAN] Defects in CTSC are a cause of Papillon-Lefevre syndrome (PLS) [MIM:[https://omim.org/entry/245000 245000]; also known as keratosis palmoplantaris with periodontopathia. PLS is an autosomal recessive disorder characterized by palmoplantar keratosis and severe periodontitis affecting deciduous and permanent dentitions and resulting in premature tooth loss. The palmoplantar keratotic phenotype vary from mild psoriasiform scaly skin to overt hyperkeratosis. Keratosis also affects other sites such as elbows and knees.<ref>PMID:11180601</ref> <ref>PMID:12809647</ref> <ref>PMID:10581027</ref> <ref>PMID:10662808</ref> <ref>PMID:11106356</ref> <ref>PMID:11180012</ref> <ref>PMID:11886537</ref> <ref>PMID:11158173</ref> <ref>PMID:12112662</ref> <ref>PMID:14974080</ref> <ref>PMID:15108292</ref> <ref>PMID:15991336</ref> Defects in CTSC are a cause of Haim-Munk syndrome (HMS) [MIM:[https://omim.org/entry/245010 245010]; also known as keratosis palmoplantaris with periodontopathia and onychogryposis or Cochin Jewish disorder. HMS is an autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis.<ref>PMID:10662807</ref> Defects in CTSC are a cause of aggressive periodontititis type 1 (AP1) [MIM:[https://omim.org/entry/170650 170650]; also known as juvenile periodontitis (JPD) and prepubertal periodontitis (PPP). AP1 is characterized by severe and protracted gingival infections, leading to tooth loss. AP1 inheritance is autosomal dominant.<ref>PMID:10662808</ref> <ref>PMID:14974080</ref>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/CATC_HUMAN CATC_HUMAN]] Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII.<ref>PMID:1586157</ref>		[https://www.uniprot.org/uniprot/CATC_HUMAN CATC_HUMAN] Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII.<ref>PMID:1586157</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			A lead generation and optimization program delivered the highly selective and potent CatC inhibitor 10 as an in vivo tool compound and potential development candidate. Structural studies were undertaken to generate SAR understanding.

			Cathepsin C Inhibitors: Property Optimization and Identification of a Clinical Candidate.,Furber M, Tiden AK, Gardiner P, Mete A, Ford R, Millichip I, Stein L, Mather A, Kinchin E, Luckhurst C, Barber S, Cage P, Sanganee H, Austin R, Chohan K, Beri R, Thong B, Wallace A, Oreffo V, Hutchinson R, Harper S, Debreczeni J, Breed J, Wissler L, Edman K J Med Chem. 2014 Mar 14. PMID:24592859<ref>PMID:24592859</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 4cdc" style="background-color:#fffaf0;"></div>

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

OCA at 17:40, 7 September 2022

2022-09-07T17:40:05Z

← Older revision		Revision as of 17:40, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4cdc' size='340' side='right'caption='[[4cdc]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='4cdc' size='340' side='right'caption='[[4cdc]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cdc]] is a 12 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=4CDC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4CDC FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cdc]] is a 12 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=4CDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CDC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6AO:(2S)-2-AZANYL-N-[(2S)-1-AZANYLIDENE-3-(4-PHENYLPHENYL)PROPAN-2-YL]BUTANAMIDE'>6AO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene~~></td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6AO:(2S)-2-AZANYL-N-[(2S)-1-AZANYLIDENE-3-(4-PHENYLPHENYL)PROPAN-2-YL]BUTANAMIDE'>6AO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cdd\|4cdd]], [[4cde\|4cde]], [[4cdf\|4cdf]]</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=4cdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cdc OCA], [https://pdbe.org/4cdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cdc RCSB], [https://www.ebi.ac.uk/pdbsum/4cdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cdc ProSAT]</span></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_I Dipeptidyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.1 3.4.14.1] </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=4cdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cdc OCA], [~~http~~://pdbe.org/4cdc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4cdc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4cdc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4cdc ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/CATC_HUMAN CATC_HUMAN]] Defects in CTSC are a cause of Papillon-Lefevre syndrome (PLS) [MIM:[~~http~~://omim.org/entry/245000 245000]]; also known as keratosis palmoplantaris with periodontopathia. PLS is an autosomal recessive disorder characterized by palmoplantar keratosis and severe periodontitis affecting deciduous and permanent dentitions and resulting in premature tooth loss. The palmoplantar keratotic phenotype vary from mild psoriasiform scaly skin to overt hyperkeratosis. Keratosis also affects other sites such as elbows and knees.<ref>PMID:11180601</ref> <ref>PMID:12809647</ref> <ref>PMID:10581027</ref> <ref>PMID:10662808</ref> <ref>PMID:11106356</ref> <ref>PMID:11180012</ref> <ref>PMID:11886537</ref> <ref>PMID:11158173</ref> <ref>PMID:12112662</ref> <ref>PMID:14974080</ref> <ref>PMID:15108292</ref> <ref>PMID:15991336</ref> Defects in CTSC are a cause of Haim-Munk syndrome (HMS) [MIM:[~~http~~://omim.org/entry/245010 245010]]; also known as keratosis palmoplantaris with periodontopathia and onychogryposis or Cochin Jewish disorder. HMS is an autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis.<ref>PMID:10662807</ref> Defects in CTSC are a cause of aggressive periodontititis type 1 (AP1) [MIM:[~~http~~://omim.org/entry/170650 170650]]; also known as juvenile periodontitis (JPD) and prepubertal periodontitis (PPP). AP1 is characterized by severe and protracted gingival infections, leading to tooth loss. AP1 inheritance is autosomal dominant.<ref>PMID:10662808</ref> <ref>PMID:14974080</ref>		[[https://www.uniprot.org/uniprot/CATC_HUMAN CATC_HUMAN]] Defects in CTSC are a cause of Papillon-Lefevre syndrome (PLS) [MIM:[https://omim.org/entry/245000 245000]]; also known as keratosis palmoplantaris with periodontopathia. PLS is an autosomal recessive disorder characterized by palmoplantar keratosis and severe periodontitis affecting deciduous and permanent dentitions and resulting in premature tooth loss. The palmoplantar keratotic phenotype vary from mild psoriasiform scaly skin to overt hyperkeratosis. Keratosis also affects other sites such as elbows and knees.<ref>PMID:11180601</ref> <ref>PMID:12809647</ref> <ref>PMID:10581027</ref> <ref>PMID:10662808</ref> <ref>PMID:11106356</ref> <ref>PMID:11180012</ref> <ref>PMID:11886537</ref> <ref>PMID:11158173</ref> <ref>PMID:12112662</ref> <ref>PMID:14974080</ref> <ref>PMID:15108292</ref> <ref>PMID:15991336</ref> Defects in CTSC are a cause of Haim-Munk syndrome (HMS) [MIM:[https://omim.org/entry/245010 245010]]; also known as keratosis palmoplantaris with periodontopathia and onychogryposis or Cochin Jewish disorder. HMS is an autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis.<ref>PMID:10662807</ref> Defects in CTSC are a cause of aggressive periodontititis type 1 (AP1) [MIM:[https://omim.org/entry/170650 170650]]; also known as juvenile periodontitis (JPD) and prepubertal periodontitis (PPP). AP1 is characterized by severe and protracted gingival infections, leading to tooth loss. AP1 inheritance is autosomal dominant.<ref>PMID:10662808</ref> <ref>PMID:14974080</ref>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/CATC_HUMAN CATC_HUMAN]] Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII.<ref>PMID:1586157</ref>		[[https://www.uniprot.org/uniprot/CATC_HUMAN CATC_HUMAN]] Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII.<ref>PMID:1586157</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	A lead generation and optimization program delivered the highly selective and potent CatC inhibitor 10 as an in vivo tool compound and potential development candidate. Structural studies were undertaken to generate SAR understanding.

	Cathepsin C Inhibitors: Property Optimization and Identification of a Clinical Candidate.,Furber M, Tiden AK, Gardiner P, Mete A, Ford R, Millichip I, Stein L, Mather A, Kinchin E, Luckhurst C, Barber S, Cage P, Sanganee H, Austin R, Chohan K, Beri R, Thong B, Wallace A, Oreffo V, Hutchinson R, Harper S, Debreczeni J, Breed J, Wissler L, Edman K J Med Chem. 2014 Mar 14. PMID:24592859<ref>PMID:24592859</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4cdc" style="background-color:#fffaf0;"></div~~>

	==See Also==		==See Also==
	*[[Cathepsin\|Cathepsin]]		*[[Cathepsin 3D structures\|Cathepsin 3D structures]]
	*[[Dipeptidyl peptidase\|Dipeptidyl peptidase]]		*[[Dipeptidyl peptidase\|Dipeptidyl peptidase]]
	== References ==		== References ==
Line 30:		Line 19:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Dipeptidyl-peptidase I]]~~		[[Category: Homo sapiens]]
	~~[[Category: Human~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Breed, J]]		[[Category: Breed J]]
	[[Category: Cage, P]]		[[Category: Cage P]]
	[[Category: Debreczeni, J]]		[[Category: Debreczeni J]]
	[[Category: Edman, K]]		[[Category: Edman K]]
	[[Category: Ford, R]]		[[Category: Ford R]]
	[[Category: Furber, M]]		[[Category: Furber M]]
	[[Category: Gardiner, P]]		[[Category: Gardiner P]]
	[[Category: Kinchin, E]]		[[Category: Kinchin E]]
	[[Category: Luckhurst, C]]		[[Category: Luckhurst C]]
	[[Category: Mather, A]]		[[Category: Mather A]]
	[[Category: Mete, T]]		[[Category: Mete T]]
	[[Category: Millichip, I]]		[[Category: Millichip I]]
	[[Category: Sanghanee, H]]		[[Category: Sanghanee H]]
	[[Category: Stein, L]]		[[Category: Stein L]]
	[[Category: Tiden, A]]		[[Category: Tiden A]]
	[[Category: Wissler, L]]		[[Category: Wissler L]]
	~~[[Category: Hydrolase]]~~
	~~[[Category: Inhibitor~~]]

OCA at 08:53, 20 March 2019

2019-03-20T08:53:05Z

← Older revision		Revision as of 08:53, 20 March 2019
Line 1:		Line 1:

	==Human DPP1 in complex with (2S)-2-amino-N-((1S)-1-cyano-2-(4- phenylphenyl)ethyl)butanamide==		==Human DPP1 in complex with (2S)-2-amino-N-((1S)-1-cyano-2-(4- phenylphenyl)ethyl)butanamide==
	<StructureSection load='4cdc' size='340' side='right' caption='[[4cdc]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='4cdc' size='340' side='right'caption='[[4cdc]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cdc]] is a 12 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=4CDC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CDC FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cdc]] is a 12 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=4CDC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CDC FirstGlance]. <br>
Line 24:		Line 24:

	==See Also==		==See Also==
			*[[Cathepsin\|Cathepsin]]
	*[[Dipeptidyl peptidase\|Dipeptidyl peptidase]]		*[[Dipeptidyl peptidase\|Dipeptidyl peptidase]]
	== References ==		== References ==
Line 31:		Line 32:
	[[Category: Dipeptidyl-peptidase I]]		[[Category: Dipeptidyl-peptidase I]]
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Breed, J]]		[[Category: Breed, J]]
	[[Category: Cage, P]]		[[Category: Cage, P]]

OCA at 14:15, 11 August 2016

2016-08-11T14:15:51Z

← Older revision		Revision as of 14:15, 11 August 2016
Line 1:		Line 1:

	==Human DPP1 in complex with (2S)-2-amino-N-((1S)-1-cyano-2-(4- phenylphenyl)ethyl)butanamide==		==Human DPP1 in complex with (2S)-2-amino-N-((1S)-1-cyano-2-(4- phenylphenyl)ethyl)butanamide==
	<StructureSection load='4cdc' size='340' side='right' caption='[[4cdc]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='4cdc' size='340' side='right' caption='[[4cdc]], [[Resolution\|resolution]] 2.40Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cdd\|4cdd]], [[4cde\|4cde]], [[4cdf\|4cdf]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cdd\|4cdd]], [[4cde\|4cde]], [[4cdf\|4cdf]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_I Dipeptidyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.1 3.4.14.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_I Dipeptidyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.1 3.4.14.1] </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=4cdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cdc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cdc RCSB], [http://www.ebi.ac.uk/pdbsum/4cdc 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=4cdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cdc OCA], [http://pdbe.org/4cdc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cdc RCSB], [http://www.ebi.ac.uk/pdbsum/4cdc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cdc ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	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 4cdc" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Dipeptidyl peptidase\|Dipeptidyl peptidase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:23, 4 January 2015

2015-01-04T12:23:30Z

← Older revision		Revision as of 12:23, 4 January 2015
Line 1:		Line 1:
	~~{{STRUCTURE_4cdc\| PDB=4cdc \| SCENE= }}~~		==Human DPP1 in complex with (2S)-2-amino-N-((1S)-1-cyano-2-(4- phenylphenyl)ethyl)butanamide==
	===Human DPP1 in complex with (2S)-2-amino-N-((1S)-1-cyano-2-(4- phenylphenyl)ethyl)butanamide===		<StructureSection load='4cdc' size='340' side='right' caption='[[4cdc]], [[Resolution\|resolution]] 2.40Å' scene=''>
	~~{{ABSTRACT_PUBMED_24592859}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4cdc]] is a 12 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=4CDC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CDC FirstGlance]. <br>
	==Disease==		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6AO:(2S)-2-AZANYL-N-[(2S)-1-AZANYLIDENE-3-(4-PHENYLPHENYL)PROPAN-2-YL]BUTANAMIDE'>6AO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cdd\|4cdd]], [[4cde\|4cde]], [[4cdf\|4cdf]]</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_I Dipeptidyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.1 3.4.14.1] </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=4cdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cdc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cdc RCSB], [http://www.ebi.ac.uk/pdbsum/4cdc PDBsum]</span></td></tr>
			</table>
			== Disease ==
	[[http://www.uniprot.org/uniprot/CATC_HUMAN CATC_HUMAN]] Defects in CTSC are a cause of Papillon-Lefevre syndrome (PLS) [MIM:[http://omim.org/entry/245000 245000]]; also known as keratosis palmoplantaris with periodontopathia. PLS is an autosomal recessive disorder characterized by palmoplantar keratosis and severe periodontitis affecting deciduous and permanent dentitions and resulting in premature tooth loss. The palmoplantar keratotic phenotype vary from mild psoriasiform scaly skin to overt hyperkeratosis. Keratosis also affects other sites such as elbows and knees.<ref>PMID:11180601</ref> <ref>PMID:12809647</ref> <ref>PMID:10581027</ref> <ref>PMID:10662808</ref> <ref>PMID:11106356</ref> <ref>PMID:11180012</ref> <ref>PMID:11886537</ref> <ref>PMID:11158173</ref> <ref>PMID:12112662</ref> <ref>PMID:14974080</ref> <ref>PMID:15108292</ref> <ref>PMID:15991336</ref> Defects in CTSC are a cause of Haim-Munk syndrome (HMS) [MIM:[http://omim.org/entry/245010 245010]]; also known as keratosis palmoplantaris with periodontopathia and onychogryposis or Cochin Jewish disorder. HMS is an autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis.<ref>PMID:10662807</ref> Defects in CTSC are a cause of aggressive periodontititis type 1 (AP1) [MIM:[http://omim.org/entry/170650 170650]]; also known as juvenile periodontitis (JPD) and prepubertal periodontitis (PPP). AP1 is characterized by severe and protracted gingival infections, leading to tooth loss. AP1 inheritance is autosomal dominant.<ref>PMID:10662808</ref> <ref>PMID:14974080</ref>		[[http://www.uniprot.org/uniprot/CATC_HUMAN CATC_HUMAN]] Defects in CTSC are a cause of Papillon-Lefevre syndrome (PLS) [MIM:[http://omim.org/entry/245000 245000]]; also known as keratosis palmoplantaris with periodontopathia. PLS is an autosomal recessive disorder characterized by palmoplantar keratosis and severe periodontitis affecting deciduous and permanent dentitions and resulting in premature tooth loss. The palmoplantar keratotic phenotype vary from mild psoriasiform scaly skin to overt hyperkeratosis. Keratosis also affects other sites such as elbows and knees.<ref>PMID:11180601</ref> <ref>PMID:12809647</ref> <ref>PMID:10581027</ref> <ref>PMID:10662808</ref> <ref>PMID:11106356</ref> <ref>PMID:11180012</ref> <ref>PMID:11886537</ref> <ref>PMID:11158173</ref> <ref>PMID:12112662</ref> <ref>PMID:14974080</ref> <ref>PMID:15108292</ref> <ref>PMID:15991336</ref> Defects in CTSC are a cause of Haim-Munk syndrome (HMS) [MIM:[http://omim.org/entry/245010 245010]]; also known as keratosis palmoplantaris with periodontopathia and onychogryposis or Cochin Jewish disorder. HMS is an autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis.<ref>PMID:10662807</ref> Defects in CTSC are a cause of aggressive periodontititis type 1 (AP1) [MIM:[http://omim.org/entry/170650 170650]]; also known as juvenile periodontitis (JPD) and prepubertal periodontitis (PPP). AP1 is characterized by severe and protracted gingival infections, leading to tooth loss. AP1 inheritance is autosomal dominant.<ref>PMID:10662808</ref> <ref>PMID:14974080</ref>
			== Function ==
	==Function==
	[[http://www.uniprot.org/uniprot/CATC_HUMAN CATC_HUMAN]] Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII.<ref>PMID:1586157</ref>		[[http://www.uniprot.org/uniprot/CATC_HUMAN CATC_HUMAN]] Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII.<ref>PMID:1586157</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			A lead generation and optimization program delivered the highly selective and potent CatC inhibitor 10 as an in vivo tool compound and potential development candidate. Structural studies were undertaken to generate SAR understanding.

	~~==About this Structure==~~		Cathepsin C Inhibitors: Property Optimization and Identification of a Clinical Candidate.,Furber M, Tiden AK, Gardiner P, Mete A, Ford R, Millichip I, Stein L, Mather A, Kinchin E, Luckhurst C, Barber S, Cage P, Sanganee H, Austin R, Chohan K, Beri R, Thong B, Wallace A, Oreffo V, Hutchinson R, Harper S, Debreczeni J, Breed J, Wissler L, Edman K J Med Chem. 2014 Mar 14. PMID:24592859<ref>PMID:24592859</ref>
	~~[[4cdc]] is~~ a ~~12 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il/oca-bin~~/~~ocashort?id=4CDC OCA].~~

	==~~Reference~~==		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~<ref group="xtra">PMID:024592859</ref>~~<references ~~group="xtra"~~/><~~references~~/>		</div>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
	[[Category: Dipeptidyl-peptidase I]]		[[Category: Dipeptidyl-peptidase I]]
	[[Category: Breed, J.]]		[[Category: Human]]
	[[Category: Cage, P.]]		[[Category: Breed, J]]
	[[Category: Debreczeni, J.]]		[[Category: Cage, P]]
	[[Category: Edman, K.]]		[[Category: Debreczeni, J]]
	[[Category: Ford, R.]]		[[Category: Edman, K]]
	[[Category: Furber, M.]]		[[Category: Ford, R]]
	[[Category: Gardiner, P.]]		[[Category: Furber, M]]
	[[Category: Kinchin, E.]]		[[Category: Gardiner, P]]
	[[Category: Luckhurst, C.]]		[[Category: Kinchin, E]]
	[[Category: Mather, A.]]		[[Category: Luckhurst, C]]
	[[Category: Mete, T.]]		[[Category: Mather, A]]
	[[Category: Millichip, I.]]		[[Category: Mete, T]]
	[[Category: Sanghanee, H.]]		[[Category: Millichip, I]]
	[[Category: Stein, L.]]		[[Category: Sanghanee, H]]
	[[Category: Tiden, A.]]		[[Category: Stein, L]]
	[[Category: Wissler, L.]]		[[Category: Tiden, A]]
			[[Category: Wissler, L]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Inhibitor]]		[[Category: Inhibitor]]

OCA at 09:04, 19 March 2014

2014-03-19T09:04:38Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{STRUCTURE_4cdc|  PDB=4cdc  |  SCENE=  }}
-The entry 4cdc is ON HOLD
+==Disease==
-Authors: Debreczeni, J., Edman, K., Furber, M., Tiden, A., Gardiner, P., Mete, T., Ford, R., Millichip, I., Stein, L., Mather, A., Kinchin, E., Luckhurst, C., Cage, P., Sanghanee, H., Breed, J., Wissler, L.
+==Function==
-Description: Human DPP1 in complex with (2S)-2-amino-N-((1S)-1-cyano-2-(4-phenylphenyl)ethyl)butanamide
+==About this Structure==

OCA: Protected "4cdc" [edit=sysop:move=sysop]

2013-11-13T07:14:25Z

Protected "4cdc" [edit=sysop:move=sysop]

← Older revision	Revision as of 07:14, 13 November 2013
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4cdc is ON HOLD Authors: Debreczeni, J., Edman, K., Furber, M., Tiden, A., Gardiner, P., Mete, T., Ford, R., Millichip, I., Stein, L., Mather, A., K...

2013-11-13T07:14:23Z

New page: '''Unreleased structure''' The entry 4cdc is ON HOLD Authors: Debreczeni, J., Edman, K., Furber, M., Tiden, A., Gardiner, P., Mete, T., Ford, R., Millichip, I., Stein, L., Mather, A., K...

New page

'''Unreleased structure'''

The entry 4cdc is ON HOLD

Authors: Debreczeni, J., Edman, K., Furber, M., Tiden, A., Gardiner, P., Mete, T., Ford, R., Millichip, I., Stein, L., Mather, A., Kinchin, E., Luckhurst, C., Cage, P., Sanghanee, H., Breed, J., Wissler, L.

Description: Human DPP1 in complex with (2S)-2-amino-N-((1S)-1-cyano-2-(4-phenylphenyl)ethyl)butanamide