4f8k - Revision history

OCA at 15:18, 14 March 2024

OCA — Thu, 14 Mar 2024 15:18:56 GMT

←Older revision		Revision as of 15:18, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4f8k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F8K FirstGlance]. <br>		<table><tr><td colspan='2'>[[4f8k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F8K FirstGlance]. <br>
-	</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=4f8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f8k OCA], [https://pdbe.org/4f8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f8k RCSB], [https://www.ebi.ac.uk/pdbsum/4f8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f8k ProSAT]</span></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]] 1.7Å</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=4f8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f8k OCA], [https://pdbe.org/4f8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f8k RCSB], [https://www.ebi.ac.uk/pdbsum/4f8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f8k ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/NHRF3_MOUSE NHRF3_MOUSE] A scaffold protein that connects plasma membrane proteins and regulatory components, regulating their surface expression in epithelial cells apical domains. May be involved in the coordination of a diverse range of regulatory processes for ion transport and second messenger cascades. In complex with SLC9A3R1, may cluster proteins that are functionally dependent in a mutual fashion and modulate the trafficking and the activity of the associated membrane proteins. May play a role in the cellular mechanisms associated with multidrug resistance through its interaction with ABCC2 and PDZK1IP1. May potentiate the CFTR chloride channel activity. May function to connect SCARB1 with the cellular machineries for intracellular cholesterol transport and/or metabolism (By similarity). May be involved in the regulation of proximal tubular Na(+)-dependent inorganic phosphate cotransport therefore playing an important role in tubule function.<ref>PMID:11051556</ref> <ref>PMID:12556478</ref> <ref>PMID:14531806</ref> <ref>PMID:15523054</ref> [https://www.uniprot.org/uniprot/PI2R_MOUSE PI2R_MOUSE] Receptor for prostacyclin (prostaglandin I2 or PGI2). The activity of this receptor is mediated by G(s) proteins which activate adenylate cyclase.		[https://www.uniprot.org/uniprot/NHRF3_MOUSE NHRF3_MOUSE] A scaffold protein that connects plasma membrane proteins and regulatory components, regulating their surface expression in epithelial cells apical domains. May be involved in the coordination of a diverse range of regulatory processes for ion transport and second messenger cascades. In complex with SLC9A3R1, may cluster proteins that are functionally dependent in a mutual fashion and modulate the trafficking and the activity of the associated membrane proteins. May play a role in the cellular mechanisms associated with multidrug resistance through its interaction with ABCC2 and PDZK1IP1. May potentiate the CFTR chloride channel activity. May function to connect SCARB1 with the cellular machineries for intracellular cholesterol transport and/or metabolism (By similarity). May be involved in the regulation of proximal tubular Na(+)-dependent inorganic phosphate cotransport therefore playing an important role in tubule function.<ref>PMID:11051556</ref> <ref>PMID:12556478</ref> <ref>PMID:14531806</ref> <ref>PMID:15523054</ref> [https://www.uniprot.org/uniprot/PI2R_MOUSE PI2R_MOUSE] Receptor for prostacyclin (prostaglandin I2 or PGI2). The activity of this receptor is mediated by G(s) proteins which activate adenylate cyclase.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The prostanoid prostacyclin, or prostaglandin I, plays an essential role in many aspects of cardiovascular disease. The actions of prostacyclin are mainly mediated through its activation of the prostacyclin receptor or, in short, the IP. In recent studies, the cytoplasmic carboxy-terminal domain of the IP was shown to bind several PDZ domains of the multi-PDZ adaptor PDZK1. The interaction between the two proteins was found to enhance cell surface expression of the IP and to be functionally important in promoting prostacyclin-induced endothelial cell migration and angiogenesis. To investigate the interaction of the IP with the first PDZ domain (PDZ1) of PDZK1, we generated a nine residue peptide (KKIAACSLC) containing the seven carboxy-terminal amino acids of the IP and measured its binding affinity to a recombinant protein corresponding to PDZ1 by isothermal titration calorimetry. We determined that the IP interacts with PDZ1 with a binding affinity of 8.2 microM. Using the same technique, we also determined that the farnesylated form of carboxy-terminus of the IP does not bind to PDZ1. To understand the molecular basis of these findings, we solved the high resolution crystal structure of PDZ1 bound to a 7-residue peptide derived from the carboxy-terminus of the non-farnesylated form of IP (IAACSLC). Analysis of the structure demonstrates a critical role for the three carboxy-terminal amino acids in establishing a strong interaction with PDZ1 and explains the inability of the farnesylated form of IP to interact with the PDZ1 domain of PDZK1 at least .
-
-	Molecular Analysis of the Prostacyclin Receptor's Interaction with the PDZ1 Domain of Its Adaptor Protein PDZK1.,Birrane G, Mulvaney EP, Pal R, Kinsella BT, Kocher O PLoS One. 2013;8(2):e53819. doi: 10.1371/journal.pone.0053819. Epub 2013 Feb 6. PMID:23457445<ref>PMID:23457445</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4f8k" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[Sodium-hydrogen exchange regulatory factor\|Sodium-hydrogen exchange regulatory factor]]	+	*[[Sodium-hydrogen exchange regulatory factor 3D structures\|Sodium-hydrogen exchange regulatory factor 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 04:41, 7 October 2022

OCA — Fri, 07 Oct 2022 04:41:19 GMT

←Older revision		Revision as of 04:41, 7 October 2022
Line 1:		Line 1:

	==Molecular analysis of the interaction between the prostacyclin receptor and the first PDZ domain of PDZK1==		==Molecular analysis of the interaction between the prostacyclin receptor and the first PDZ domain of PDZK1==
-	<StructureSection load='4f8k' size='340' side='right' caption='[[4f8k]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='4f8k' size='340' side='right'caption='[[4f8k]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4f8k]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F8K OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4F8K FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4f8k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F8K FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ngh\|3ngh]]</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=4f8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f8k OCA], [https://pdbe.org/4f8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f8k RCSB], [https://www.ebi.ac.uk/pdbsum/4f8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f8k ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Cap70, Nherf3, Pdzk1, Prostacyclin receptor, Ptgir ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4f8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f8k OCA], [~~http~~://pdbe.org/4f8k PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4f8k RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4f8k PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4f8k ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/NHRF3_MOUSE NHRF3_MOUSE]] A scaffold protein that connects plasma membrane proteins and regulatory components, regulating their surface expression in epithelial cells apical domains. May be involved in the coordination of a diverse range of regulatory processes for ion transport and second messenger cascades. In complex with SLC9A3R1, may cluster proteins that are functionally dependent in a mutual fashion and modulate the trafficking and the activity of the associated membrane proteins. May play a role in the cellular mechanisms associated with multidrug resistance through its interaction with ABCC2 and PDZK1IP1. May potentiate the CFTR chloride channel activity. May function to connect SCARB1 with the cellular machineries for intracellular cholesterol transport and/or metabolism (By similarity). May be involved in the regulation of proximal tubular Na(+)-dependent inorganic phosphate cotransport therefore playing an important role in tubule function.<ref>PMID:11051556</ref> <ref>PMID:12556478</ref> <ref>PMID:14531806</ref> <ref>PMID:15523054</ref>	+	[https://www.uniprot.org/uniprot/NHRF3_MOUSE NHRF3_MOUSE] A scaffold protein that connects plasma membrane proteins and regulatory components, regulating their surface expression in epithelial cells apical domains. May be involved in the coordination of a diverse range of regulatory processes for ion transport and second messenger cascades. In complex with SLC9A3R1, may cluster proteins that are functionally dependent in a mutual fashion and modulate the trafficking and the activity of the associated membrane proteins. May play a role in the cellular mechanisms associated with multidrug resistance through its interaction with ABCC2 and PDZK1IP1. May potentiate the CFTR chloride channel activity. May function to connect SCARB1 with the cellular machineries for intracellular cholesterol transport and/or metabolism (By similarity). May be involved in the regulation of proximal tubular Na(+)-dependent inorganic phosphate cotransport therefore playing an important role in tubule function.<ref>PMID:11051556</ref> <ref>PMID:12556478</ref> <ref>PMID:14531806</ref> <ref>PMID:15523054</ref> [https://www.uniprot.org/uniprot/PI2R_MOUSE PI2R_MOUSE] Receptor for prostacyclin (prostaglandin I2 or PGI2). The activity of this receptor is mediated by G(s) proteins which activate adenylate cyclase.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 17:
	</div>		</div>
	<div class="pdbe-citations 4f8k" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4f8k" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Sodium-hydrogen exchange regulatory factor\|Sodium-hydrogen exchange regulatory factor]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Birrane, G~~]]	+	[[Category: Mus musculus]]
-	[[Category: ~~Kinsella, B T~~]]	+	[[Category: Birrane G]]
-	[[Category: ~~Kocher, O~~]]	+	[[Category: Kinsella BT]]
-	[[Category: ~~Mulvaney, E P~~]]	+	[[Category: Kocher O]]
-	[[Category: ~~Adaptor protein]]~~	+	[[Category: Mulvaney EP]]
-	~~[[Category: Chimera protein]]~~	+
-	~~[[Category: Fusion protein]]~~	+
-	~~[[Category: Pdz domain]]~~	+
-	~~[[Category: Prostacyclin receptor]]~~	+
-	~~[[Category: Signaling protein~~]]	+

OCA at 13:02, 5 August 2016

OCA — Fri, 05 Aug 2016 13:02:37 GMT

←Older revision		Revision as of 13:02, 5 August 2016
Line 1:		Line 1:
		+
	==Molecular analysis of the interaction between the prostacyclin receptor and the first PDZ domain of PDZK1==		==Molecular analysis of the interaction between the prostacyclin receptor and the first PDZ domain of PDZK1==
	<StructureSection load='4f8k' size='340' side='right' caption='[[4f8k]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='4f8k' size='340' side='right' caption='[[4f8k]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4f8k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F8K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F8K FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4f8k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F8K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F8K FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ngh\|3ngh]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ngh\|3ngh]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Cap70, Nherf3, Pdzk1, Prostacyclin receptor, Ptgir ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 ~~Mus musculus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Cap70, Nherf3, Pdzk1, Prostacyclin receptor, Ptgir ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4f8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f8k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f8k RCSB], [http://www.ebi.ac.uk/pdbsum/4f8k 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=4f8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f8k OCA], [http://pdbe.org/4f8k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f8k RCSB], [http://www.ebi.ac.uk/pdbsum/4f8k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f8k ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4f8k" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Mus musculus~~]]	+	[[Category: Lk3 transgenic mice]]
	[[Category: Birrane, G]]		[[Category: Birrane, G]]
	[[Category: Kinsella, B T]]		[[Category: Kinsella, B T]]

OCA at 19:03, 25 December 2014

OCA — Thu, 25 Dec 2014 19:03:39 GMT

←Older revision		Revision as of 19:03, 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=4f8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f8k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f8k RCSB], [http://www.ebi.ac.uk/pdbsum/4f8k 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=4f8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f8k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f8k RCSB], [http://www.ebi.ac.uk/pdbsum/4f8k PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NHRF3_MOUSE NHRF3_MOUSE]] A scaffold protein that connects plasma membrane proteins and regulatory components, regulating their surface expression in epithelial cells apical domains. May be involved in the coordination of a diverse range of regulatory processes for ion transport and second messenger cascades. In complex with SLC9A3R1, may cluster proteins that are functionally dependent in a mutual fashion and modulate the trafficking and the activity of the associated membrane proteins. May play a role in the cellular mechanisms associated with multidrug resistance through its interaction with ABCC2 and PDZK1IP1. May potentiate the CFTR chloride channel activity. May function to connect SCARB1 with the cellular machineries for intracellular cholesterol transport and/or metabolism (By similarity). May be involved in the regulation of proximal tubular Na(+)-dependent inorganic phosphate cotransport therefore playing an important role in tubule function.<ref>PMID:11051556</ref> <ref>PMID:12556478</ref> <ref>PMID:14531806</ref> <ref>PMID:15523054</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 10:46, 21 December 2014

OCA — Sun, 21 Dec 2014 10:46:49 GMT

←Older revision		Revision as of 10:46, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4f8k\| PDB=4f8k \| SCENE= }}~~	+	==Molecular analysis of the interaction between the prostacyclin receptor and the first PDZ domain of PDZK1==
-	===Molecular analysis of the interaction between the prostacyclin receptor and the first PDZ domain of PDZK1===	+	<StructureSection load='4f8k' size='340' side='right' caption='[[4f8k]], [[Resolution\|resolution]] 1.70Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23457445}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4f8k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F8K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F8K FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ngh\|3ngh]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Cap70, Nherf3, Pdzk1, Prostacyclin receptor, Ptgir ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=4f8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f8k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f8k RCSB], [http://www.ebi.ac.uk/pdbsum/4f8k PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The prostanoid prostacyclin, or prostaglandin I, plays an essential role in many aspects of cardiovascular disease. The actions of prostacyclin are mainly mediated through its activation of the prostacyclin receptor or, in short, the IP. In recent studies, the cytoplasmic carboxy-terminal domain of the IP was shown to bind several PDZ domains of the multi-PDZ adaptor PDZK1. The interaction between the two proteins was found to enhance cell surface expression of the IP and to be functionally important in promoting prostacyclin-induced endothelial cell migration and angiogenesis. To investigate the interaction of the IP with the first PDZ domain (PDZ1) of PDZK1, we generated a nine residue peptide (KKIAACSLC) containing the seven carboxy-terminal amino acids of the IP and measured its binding affinity to a recombinant protein corresponding to PDZ1 by isothermal titration calorimetry. We determined that the IP interacts with PDZ1 with a binding affinity of 8.2 microM. Using the same technique, we also determined that the farnesylated form of carboxy-terminus of the IP does not bind to PDZ1. To understand the molecular basis of these findings, we solved the high resolution crystal structure of PDZ1 bound to a 7-residue peptide derived from the carboxy-terminus of the non-farnesylated form of IP (IAACSLC). Analysis of the structure demonstrates a critical role for the three carboxy-terminal amino acids in establishing a strong interaction with PDZ1 and explains the inability of the farnesylated form of IP to interact with the PDZ1 domain of PDZK1 at least .

-	~~==Function==~~	+	Molecular Analysis of the Prostacyclin Receptor's Interaction with the PDZ1 Domain of Its Adaptor Protein PDZK1.,Birrane G, Mulvaney EP, Pal R, Kinsella BT, Kocher O PLoS One. 2013;8(2):e53819. doi: 10.1371/journal.pone.0053819. Epub 2013 Feb 6. PMID:23457445<ref>PMID:23457445</ref>
-	[[http://www.uniprot.org/uniprot/NHRF3_MOUSE NHRF3_MOUSE]] A scaffold protein that connects plasma membrane proteins and regulatory components, regulating their surface expression in epithelial cells apical domains. May be involved in the ~~coordination of a diverse range of regulatory processes for ion transport and second messenger cascades. In complex~~ with ~~SLC9A3R1, may cluster proteins that are functionally dependent in a mutual fashion and modulate~~ the ~~trafficking and the activity~~ of ~~the associated membrane proteins~~. ~~May play a role in the cellular mechanisms associated with multidrug resistance through its interaction with ABCC2 and PDZK1IP1~~. ~~May potentiate the CFTR chloride channel activity. May function to connect SCARB1 with the cellular machineries for intracellular cholesterol transport and/or metabolism~~ (~~By similarity~~). ~~May be involved in the regulation of proximal tubular Na(+)-dependent inorganic phosphate cotransport therefore playing an important role in tubule function~~.~~<ref>PMID:11051556<~~/~~ref><ref>~~PMID:~~12556478</ref><ref>PMID:14531806</ref>~~<ref>PMID:~~15523054~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4f8k]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Mus_musculus Mus musculus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4F8K OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Birrane, G.]]	+	[[Category: Birrane, G]]
-	[[Category: Kinsella, B T.]]	+	[[Category: Kinsella, B T]]
-	[[Category: Kocher, O.]]	+	[[Category: Kocher, O]]
-	[[Category: Mulvaney, E P.]]	+	[[Category: Mulvaney, E P]]
	[[Category: Adaptor protein]]		[[Category: Adaptor protein]]
	[[Category: Chimera protein]]		[[Category: Chimera protein]]

OCA at 07:37, 27 March 2013

OCA — Wed, 27 Mar 2013 07:37:17 GMT

←Older revision		Revision as of 07:37, 27 March 2013
Line 1:		Line 1:
-	[[Image:4f8k.jpg\|left\|200px]]
-
	{{STRUCTURE_4f8k\| PDB=4f8k \| SCENE= }}		{{STRUCTURE_4f8k\| PDB=4f8k \| SCENE= }}
-
	===Molecular analysis of the interaction between the prostacyclin receptor and the first PDZ domain of PDZK1===		===Molecular analysis of the interaction between the prostacyclin receptor and the first PDZ domain of PDZK1===
		+	{{ABSTRACT_PUBMED_23457445}}

		+	==Function==
		+	[[http://www.uniprot.org/uniprot/NHRF3_MOUSE NHRF3_MOUSE]] A scaffold protein that connects plasma membrane proteins and regulatory components, regulating their surface expression in epithelial cells apical domains. May be involved in the coordination of a diverse range of regulatory processes for ion transport and second messenger cascades. In complex with SLC9A3R1, may cluster proteins that are functionally dependent in a mutual fashion and modulate the trafficking and the activity of the associated membrane proteins. May play a role in the cellular mechanisms associated with multidrug resistance through its interaction with ABCC2 and PDZK1IP1. May potentiate the CFTR chloride channel activity. May function to connect SCARB1 with the cellular machineries for intracellular cholesterol transport and/or metabolism (By similarity). May be involved in the regulation of proximal tubular Na(+)-dependent inorganic phosphate cotransport therefore playing an important role in tubule function.<ref>PMID:11051556</ref><ref>PMID:12556478</ref><ref>PMID:14531806</ref><ref>PMID:15523054</ref>

	==About this Structure==		==About this Structure==
	[[4f8k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F8K OCA].		[[4f8k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F8K OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Birrane, G.]]		[[Category: Birrane, G.]]

OCA at 14:56, 27 February 2013

OCA — Wed, 27 Feb 2013 14:56:59 GMT

←Older revision		Revision as of 14:56, 27 February 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4f8k.jpg\|left\|200px]]

-	~~The entry~~ 4f8k ~~is ON HOLD~~	+	{{STRUCTURE_4f8k\| PDB=4f8k \| SCENE= }}

-	~~Authors: Kocher, O., Birrane, G., Kinsella, B.T., Mulvaney, E.P.~~	+	===Molecular analysis of the interaction between the prostacyclin receptor and the first PDZ domain of PDZK1===

-	~~Description~~: ~~Molecular analysis of the interaction between the prostacyclin receptor and the first PDZ~~ domain ~~of PDZK1~~	+
		+	==About this Structure==
		+	[[4f8k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F8K OCA].
		+	[[Category: Mus musculus]]
		+	[[Category: Birrane, G.]]
		+	[[Category: Kinsella, B T.]]
		+	[[Category: Kocher, O.]]
		+	[[Category: Mulvaney, E P.]]
		+	[[Category: Adaptor protein]]
		+	[[Category: Chimera protein]]
		+	[[Category: Fusion protein]]
		+	[[Category: Pdz domain]]
		+	[[Category: Prostacyclin receptor]]
		+	[[Category: Signaling protein]]

OCA at 13:16, 20 February 2013

OCA — Wed, 20 Feb 2013 13:16:23 GMT

←Older revision		Revision as of 13:16, 20 February 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4f8k is ON HOLD ~~until Paper Publication~~	+	The entry 4f8k is ON HOLD

	Authors: Kocher, O., Birrane, G., Kinsella, B.T., Mulvaney, E.P.		Authors: Kocher, O., Birrane, G., Kinsella, B.T., Mulvaney, E.P.

	Description: Molecular analysis of the interaction between the prostacyclin receptor and the first PDZ domain of PDZK1		Description: Molecular analysis of the interaction between the prostacyclin receptor and the first PDZ domain of PDZK1

OCA at 04:52, 8 August 2012

OCA — Wed, 08 Aug 2012 04:52:10 GMT

←Older revision		Revision as of 04:52, 8 August 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4f8k is ON HOLD	+	The entry 4f8k is ON HOLD until Paper Publication

	Authors: Kocher, O., Birrane, G., Kinsella, B.T., Mulvaney, E.P.		Authors: Kocher, O., Birrane, G., Kinsella, B.T., Mulvaney, E.P.

	Description: Molecular analysis of the interaction between the prostacyclin receptor and the first PDZ domain of PDZK1		Description: Molecular analysis of the interaction between the prostacyclin receptor and the first PDZ domain of PDZK1

OCA: Protected "4f8k" [edit=sysop:move=sysop]

OCA — Wed, 23 May 2012 05:45:54 GMT

Protected "4f8k" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:45, 23 May 2012