4ffv - Revision history

OCA at 13:37, 22 February 2023

OCA — Wed, 22 Feb 2023 13:37:56 GMT

←Older revision		Revision as of 13:37, 22 February 2023
Line 3:		Line 3:
	<StructureSection load='4ffv' size='340' side='right'caption='[[4ffv]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='4ffv' size='340' side='right'caption='[[4ffv]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ffv]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~] and [https://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FFV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ffv]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FFV FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Dpp4, Cd26 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>	+	</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=4ffv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ffv OCA], [https://pdbe.org/4ffv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ffv RCSB], [https://www.ebi.ac.uk/pdbsum/4ffv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ffv ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </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=4ffv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ffv OCA], [https://pdbe.org/4ffv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ffv RCSB], [https://www.ebi.ac.uk/pdbsum/4ffv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ffv ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/DPP4_RAT DPP4_RAT]] Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones (By similarity). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.	+	[https://www.uniprot.org/uniprot/DPP4_RAT DPP4_RAT] Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones (By similarity). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.

	==See Also==		==See Also==
Line 15:		Line 13:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Buffalo rat]]
-	[[Category: Dipeptidyl-peptidase IV]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Min, X]]	+	[[Category: Rattus norvegicus]]
-	[[Category: Sudom, A]]	+	[[Category: Min X]]
-	[[Category: Walker~~, N P~~]]	+	[[Category: Sudom A]]
-	[[Category: Wang, Z]]	+	[[Category: Walker NP]]
-	~~[[Category: Hydrolase]]~~	+	[[Category: Wang Z]]
-	~~[[Category: Hydrolase-immune system]]~~	+
-	~~[[Category: Inhibitor complex~~]]	+

OCA at 10:12, 19 May 2021

OCA — Wed, 19 May 2021 10:12:41 GMT

←Older revision		Revision as of 10:12, 19 May 2021
Line 1:		Line 1:

	==Crystal Structure of Dipeptidyl Peptidase IV (DPP4, DPP-IV, CD26) in Complex with 11A19 Fab==		==Crystal Structure of Dipeptidyl Peptidase IV (DPP4, DPP-IV, CD26) in Complex with 11A19 Fab==
-	<StructureSection load='4ffv' size='340' side='right' caption='[[4ffv]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='4ffv' size='340' side='right'caption='[[4ffv]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ffv]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [~~http~~://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FFV OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4FFV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ffv]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FFV FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Dpp4, Cd26 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Dpp4, Cd26 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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_IV Dipeptidyl-peptidase IV], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </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=4ffv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ffv OCA], [~~http~~://pdbe.org/4ffv PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ffv RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ffv PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ffv 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=4ffv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ffv OCA], [https://pdbe.org/4ffv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ffv RCSB], [https://www.ebi.ac.uk/pdbsum/4ffv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ffv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/DPP4_RAT DPP4_RAT]] Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones (By similarity). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.	+	[[https://www.uniprot.org/uniprot/DPP4_RAT DPP4_RAT]] Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones (By similarity). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.

	==See Also==		==See Also==
-	*[[Dipeptidyl peptidase\|Dipeptidyl peptidase]]	+	*[[Dipeptidyl peptidase 3D structures\|Dipeptidyl peptidase 3D structures]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Buffalo rat]]		[[Category: Buffalo rat]]
	[[Category: Dipeptidyl-peptidase IV]]		[[Category: Dipeptidyl-peptidase IV]]
		+	[[Category: Large Structures]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Min, X]]		[[Category: Min, X]]

OCA at 19:01, 4 August 2016

OCA — Thu, 04 Aug 2016 19:01:49 GMT

←Older revision		Revision as of 19:01, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of Dipeptidyl Peptidase IV (DPP4, DPP-IV, CD26) in Complex with 11A19 Fab==		==Crystal Structure of Dipeptidyl Peptidase IV (DPP4, DPP-IV, CD26) in Complex with 11A19 Fab==
	<StructureSection load='4ffv' size='340' side='right' caption='[[4ffv]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='4ffv' size='340' side='right' caption='[[4ffv]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ffv]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~] and [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FFV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FFV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ffv]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FFV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FFV FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Dpp4, Cd26 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 ~~Rattus norvegicus~~])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Dpp4, Cd26 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </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_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </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=4ffv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ffv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ffv RCSB], [http://www.ebi.ac.uk/pdbsum/4ffv 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=4ffv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ffv OCA], [http://pdbe.org/4ffv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ffv RCSB], [http://www.ebi.ac.uk/pdbsum/4ffv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ffv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Buffalo rat]]
	[[Category: Dipeptidyl-peptidase IV]]		[[Category: Dipeptidyl-peptidase IV]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Rattus norvegicus]]
	[[Category: Min, X]]		[[Category: Min, X]]
	[[Category: Sudom, A]]		[[Category: Sudom, A]]

OCA at 12:12, 25 December 2014

OCA — Thu, 25 Dec 2014 12:12:15 GMT

←Older revision		Revision as of 12:12, 25 December 2014
Line 7:		Line 7:
	<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=4ffv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ffv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ffv RCSB], [http://www.ebi.ac.uk/pdbsum/4ffv 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=4ffv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ffv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ffv RCSB], [http://www.ebi.ac.uk/pdbsum/4ffv PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DPP4_RAT DPP4_RAT]] Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones (By similarity). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.

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

OCA at 14:16, 9 December 2014

OCA — Tue, 09 Dec 2014 14:16:37 GMT

←Older revision		Revision as of 14:16, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4ffv.~~jpg~~\|~~left\|200px~~]]	+	==Crystal Structure of Dipeptidyl Peptidase IV (DPP4, DPP-IV, CD26) in Complex with 11A19 Fab==
		+	<StructureSection load='4ffv' size='340' side='right' caption='[[4ffv]], [[Resolution\|resolution]] 2.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4ffv]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FFV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FFV FirstGlance]. <br>
		+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Dpp4, Cd26 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</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_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </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=4ffv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ffv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ffv RCSB], [http://www.ebi.ac.uk/pdbsum/4ffv PDBsum]</span></td></tr>
		+	</table>

-	~~{{STRUCTURE_4ffv\| PDB~~=~~4ffv \| SCENE~~= }}	+	==See Also==
-		+	*[[Dipeptidyl peptidase\|Dipeptidyl peptidase]]
-	~~===Crystal Structure of Dipeptidyl Peptidase IV (DPP4, DPP-IV, CD26) in Complex with 11A19 Fab===~~	+	__TOC__
-		+	</StructureSection>
-		+
-	~~==About this Structure~~==	+
-	[[~~4ffv~~]] ~~is a 6 chain structure with sequence from [http:~~//en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FFV OCA].	+
	[[Category: Dipeptidyl-peptidase IV]]		[[Category: Dipeptidyl-peptidase IV]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Min, X.]]	+	[[Category: Min, X]]
-	[[Category: Sudom, A.]]	+	[[Category: Sudom, A]]
-	[[Category: Walker, N P.]]	+	[[Category: Walker, N P]]
-	[[Category: Wang, Z.]]	+	[[Category: Wang, Z]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Hydrolase-immune system]]		[[Category: Hydrolase-immune system]]
	[[Category: Inhibitor complex]]		[[Category: Inhibitor complex]]

OCA at 21:26, 12 December 2012

OCA — Wed, 12 Dec 2012 21:26:16 GMT

←Older revision		Revision as of 21:26, 12 December 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4ffv.jpg\|left\|200px]]

-	~~The entry~~ 4ffv ~~is ON HOLD~~ ~~until sometime in the future~~	+	{{STRUCTURE_4ffv\| PDB=4ffv \| SCENE= }}

-	~~Authors: Wang~~, Z., ~~Sudom, A., Walker, N.P.~~	+	===Crystal Structure of Dipeptidyl Peptidase IV (DPP4, DPP-IV, CD26) in Complex with 11A19 Fab===

-	~~Description: Crystal~~ Structure of Dipeptidyl ~~Peptidase IV (DPP4, DPP~~-IV, ~~CD26) in Complex with 11A19 Fab~~	+
		+	==About this Structure==
		+	[[4ffv]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FFV OCA].
		+	[[Category: Dipeptidyl-peptidase IV]]
		+	[[Category: Mus musculus]]
		+	[[Category: Rattus norvegicus]]
		+	[[Category: Min, X.]]
		+	[[Category: Sudom, A.]]
		+	[[Category: Walker, N P.]]
		+	[[Category: Wang, Z.]]
		+	[[Category: Hydrolase]]
		+	[[Category: Hydrolase-immune system]]
		+	[[Category: Inhibitor complex]]

OCA at 10:23, 5 December 2012

OCA — Wed, 05 Dec 2012 10:23:45 GMT

←Older revision		Revision as of 10:23, 5 December 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4ffv is ON HOLD until ~~Paper Publication~~	+	The entry 4ffv is ON HOLD until sometime in the future

	Authors: Wang, Z., Sudom, A., Walker, N.P.		Authors: Wang, Z., Sudom, A., Walker, N.P.

	Description: Crystal Structure of Dipeptidyl Peptidase IV (DPP4, DPP-IV, CD26) in Complex with 11A19 Fab		Description: Crystal Structure of Dipeptidyl Peptidase IV (DPP4, DPP-IV, CD26) in Complex with 11A19 Fab

OCA at 06:49, 10 October 2012

OCA — Wed, 10 Oct 2012 06:49:11 GMT

←Older revision		Revision as of 06:49, 10 October 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4ffv is ON HOLD	+	The entry 4ffv is ON HOLD until Paper Publication

	Authors: Wang, Z., Sudom, A., Walker, N.P.		Authors: Wang, Z., Sudom, A., Walker, N.P.

	Description: Crystal Structure of Dipeptidyl Peptidase IV (DPP4, DPP-IV, CD26) in Complex with 11A19 Fab		Description: Crystal Structure of Dipeptidyl Peptidase IV (DPP4, DPP-IV, CD26) in Complex with 11A19 Fab

OCA at 07:25, 20 June 2012

OCA — Wed, 20 Jun 2012 07:25:10 GMT

←Older revision		Revision as of 07:25, 20 June 2012
Line 3:		Line 3:
	The entry 4ffv is ON HOLD		The entry 4ffv is ON HOLD

-	Authors: Wang, ~~Zhulun~~, Sudom, ~~Athena~~, Walker, ~~Nigel~~ P.	+	Authors: Wang, Z., Sudom, A., Walker, N.P.

	Description: Crystal Structure of Dipeptidyl Peptidase IV (DPP4, DPP-IV, CD26) in Complex with 11A19 Fab		Description: Crystal Structure of Dipeptidyl Peptidase IV (DPP4, DPP-IV, CD26) in Complex with 11A19 Fab

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

OCA — Wed, 13 Jun 2012 05:51:07 GMT

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

←Older revision

Revision as of 05:51, 13 June 2012