4e35 - Revision history

OCA at 14:50, 14 March 2024

2024-03-14T14:50:56Z

← Older revision		Revision as of 14:50, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e35]] is a 4 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=4E35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E35 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e35]] is a 4 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=4E35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E35 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.4Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4e35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e35 OCA], [https://pdbe.org/4e35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e35 RCSB], [https://www.ebi.ac.uk/pdbsum/4e35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e35 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=4e35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e35 OCA], [https://pdbe.org/4e35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e35 RCSB], [https://www.ebi.ac.uk/pdbsum/4e35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e35 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[https://www.uniprot.org/uniprot/GOPC_HUMAN GOPC_HUMAN]] Note=A chromosomal aberration involving GOPC is found in a glioblastoma multiforme sample. An intra-chromosomal deletion del(6)(q21q21) is responsible for the formation of GOPC-ROS1 chimeric protein which has a constitutive receptor tyrosine kinase activity.<ref>PMID:12661006</ref>		[https://www.uniprot.org/uniprot/GOPC_HUMAN GOPC_HUMAN] Note=A chromosomal aberration involving GOPC is found in a glioblastoma multiforme sample. An intra-chromosomal deletion del(6)(q21q21) is responsible for the formation of GOPC-ROS1 chimeric protein which has a constitutive receptor tyrosine kinase activity.<ref>PMID:12661006</ref>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/GOPC_HUMAN GOPC_HUMAN]] Plays a role in intracellular protein trafficking and degradation. May regulate CFTR chloride currents and acid-induced ASIC3 currents by modulating cell surface expression of both channels. May also regulate the intracellular trafficking of the ADR1B receptor. May play a role in autophagy. Overexpression results in CFTR intracellular retention and degradation in the lysosomes.<ref>PMID:11707463</ref> <ref>PMID:14570915</ref> <ref>PMID:15358775</ref>		[https://www.uniprot.org/uniprot/GOPC_HUMAN GOPC_HUMAN] Plays a role in intracellular protein trafficking and degradation. May regulate CFTR chloride currents and acid-induced ASIC3 currents by modulating cell surface expression of both channels. May also regulate the intracellular trafficking of the ADR1B receptor. May play a role in autophagy. Overexpression results in CFTR intracellular retention and degradation in the lysosomes.<ref>PMID:11707463</ref> <ref>PMID:14570915</ref> <ref>PMID:15358775</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	PDZ (PSD-95/Dlg/ZO-1) binding domains often serve as cellular traffic engineers, controlling the localization and activity of a wide variety of binding partners. As a result, they play important roles in both physiological and pathological processes. However, PDZ binding specificities overlap, allowing multiple PDZ proteins to mediate distinct effects on shared binding partners. For example, several PDZ domains bind the cystic fibrosis (CF) transmembrane conductance regulator (CFTR), an epithelial ion channel mutated in CF. Among these binding partners, the CFTR-associated ligand (CAL) facilitates post-maturational degradation of the channel and is thus a potential therapeutic target. Using iterative optimization, we previously developed a selective CAL inhibitor peptide (iCAL36). Here, we investigate the stereochemical basis of iCAL36 specificity. The crystal structure of iCAL36 in complex with the CAL PDZ domain reveals stereochemical interactions distributed along the peptide-binding cleft, despite the apparent degeneracy of the CAL binding motif. A critical selectivity determinant that distinguishes CAL from other CFTR-binding PDZ domains is the accommodation of an isoleucine residue at the C-terminal position (P(0)), a characteristic shared with the Tax-interacting protein-1. Comparison of the structures of these two PDZ domains in complex with ligands containing P(0) Leu or Ile residues reveals two distinct modes of accommodation for beta-branched C-terminal side chains. Access to each mode is controlled by distinct residues in the carboxylate-binding loop. These studies provide new insights into the primary sequence determinants of binding motifs, which in turn control the scope and evolution of PDZ interactomes.

	Stereochemical Determinants of C-terminal Specificity in PDZ Peptide-binding Domains: A NOVEL CONTRIBUTION OF THE CARBOXYLATE-BINDING LOOP.,Amacher JF, Cushing PR, Bahl CD, Beck T, Madden DR J Biol Chem. 2013 Feb 15;288(7):5114-26. doi: 10.1074/jbc.M112.401588. Epub 2012 , Dec 15. PMID:23243314<ref>PMID:23243314</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4e35" style="background-color:#fffaf0;"></div~~>
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:47, 28 September 2022

2022-09-28T06:47:09Z

← Older revision		Revision as of 06:47, 28 September 2022
Line 1:		Line 1:

	==Crystal structure of CFTR Associated Ligand (CAL) PDZ domain bound to iCAL36-L (ANSRWPTSIL) peptide==		==Crystal structure of CFTR Associated Ligand (CAL) PDZ domain bound to iCAL36-L (ANSRWPTSIL) peptide==
	<StructureSection load='4e35' size='340' side='right' caption='[[4e35]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='4e35' size='340' side='right'caption='[[4e35]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e35]] is a 4 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=4E35 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4E35 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e35]] is a 4 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=4E35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E35 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>~~</td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e34\|4e34]], [[4e36\|4e36]]</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=4e35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e35 OCA], [https://pdbe.org/4e35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e35 RCSB], [https://www.ebi.ac.uk/pdbsum/4e35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e35 ProSAT]</span></td></tr>
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GOPC, CAL, FIG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</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=4e35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e35 OCA], [~~http~~://pdbe.org/4e35 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4e35 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4e35 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4e35 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/GOPC_HUMAN GOPC_HUMAN]] Note=A chromosomal aberration involving GOPC is found in a glioblastoma multiforme sample. An intra-chromosomal deletion del(6)(q21q21) is responsible for the formation of GOPC-ROS1 chimeric protein which has a constitutive receptor tyrosine kinase activity.<ref>PMID:12661006</ref>		[[https://www.uniprot.org/uniprot/GOPC_HUMAN GOPC_HUMAN]] Note=A chromosomal aberration involving GOPC is found in a glioblastoma multiforme sample. An intra-chromosomal deletion del(6)(q21q21) is responsible for the formation of GOPC-ROS1 chimeric protein which has a constitutive receptor tyrosine kinase activity.<ref>PMID:12661006</ref>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/GOPC_HUMAN GOPC_HUMAN]] Plays a role in intracellular protein trafficking and degradation. May regulate CFTR chloride currents and acid-induced ASIC3 currents by modulating cell surface expression of both channels. May also regulate the intracellular trafficking of the ADR1B receptor. May play a role in autophagy. Overexpression results in CFTR intracellular retention and degradation in the lysosomes.<ref>PMID:11707463</ref> <ref>PMID:14570915</ref> <ref>PMID:15358775</ref>		[[https://www.uniprot.org/uniprot/GOPC_HUMAN GOPC_HUMAN]] Plays a role in intracellular protein trafficking and degradation. May regulate CFTR chloride currents and acid-induced ASIC3 currents by modulating cell surface expression of both channels. May also regulate the intracellular trafficking of the ADR1B receptor. May play a role in autophagy. Overexpression results in CFTR intracellular retention and degradation in the lysosomes.<ref>PMID:11707463</ref> <ref>PMID:14570915</ref> <ref>PMID:15358775</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: ~~Amacher, J F~~]]		[[Category: Large Structures]]
	[[Category: ~~Madden, D R~~]]		[[Category: Amacher JF]]
	[[Category: ~~Pdz-peptide complex]]~~		[[Category: Madden DR]]
	~~[[Category: Protein transport-protein binding complex~~]]

OCA at 20:24, 11 August 2016

2016-08-11T20:24:01Z

← Older revision		Revision as of 20:24, 11 August 2016
Line 1:		Line 1:

	==Crystal structure of CFTR Associated Ligand (CAL) PDZ domain bound to iCAL36-L (ANSRWPTSIL) peptide==		==Crystal structure of CFTR Associated Ligand (CAL) PDZ domain bound to iCAL36-L (ANSRWPTSIL) peptide==
	<StructureSection load='4e35' size='340' side='right' caption='[[4e35]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='4e35' size='340' side='right' caption='[[4e35]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e35]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E35 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E35 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e35]] is a 4 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=4E35 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E35 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e34\|4e34]], [[4e36\|4e36]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e34\|4e34]], [[4e36\|4e36]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GOPC, CAL, FIG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GOPC, CAL, FIG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4e35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e35 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e35 RCSB], [http://www.ebi.ac.uk/pdbsum/4e35 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=4e35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e35 OCA], [http://pdbe.org/4e35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e35 RCSB], [http://www.ebi.ac.uk/pdbsum/4e35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e35 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 4e35" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Amacher, J F]]		[[Category: Amacher, J F]]
	[[Category: Madden, D R]]		[[Category: Madden, D R]]
	[[Category: Pdz-peptide complex]]		[[Category: Pdz-peptide complex]]
	[[Category: Protein transport-protein binding complex]]		[[Category: Protein transport-protein binding complex]]

OCA at 13:24, 4 January 2015

2015-01-04T13:24:01Z

← Older revision		Revision as of 13:24, 4 January 2015
Line 1:		Line 1:
	~~{{STRUCTURE_4e35\| PDB=4e35 \| SCENE= }}~~		==Crystal structure of CFTR Associated Ligand (CAL) PDZ domain bound to iCAL36-L (ANSRWPTSIL) peptide==
	===Crystal structure of CFTR Associated Ligand (CAL) PDZ domain bound to iCAL36-L (ANSRWPTSIL) peptide===		<StructureSection load='4e35' size='340' side='right' caption='[[4e35]], [[Resolution\|resolution]] 1.40Å' scene=''>
	~~{{ABSTRACT_PUBMED_23243314}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4e35]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E35 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E35 FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e34\|4e34]], [[4e36\|4e36]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GOPC, CAL, FIG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4e35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e35 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e35 RCSB], [http://www.ebi.ac.uk/pdbsum/4e35 PDBsum]</span></td></tr>
			</table>
			== Disease ==
			[[http://www.uniprot.org/uniprot/GOPC_HUMAN GOPC_HUMAN]] Note=A chromosomal aberration involving GOPC is found in a glioblastoma multiforme sample. An intra-chromosomal deletion del(6)(q21q21) is responsible for the formation of GOPC-ROS1 chimeric protein which has a constitutive receptor tyrosine kinase activity.<ref>PMID:12661006</ref>
			== Function ==
			[[http://www.uniprot.org/uniprot/GOPC_HUMAN GOPC_HUMAN]] Plays a role in intracellular protein trafficking and degradation. May regulate CFTR chloride currents and acid-induced ASIC3 currents by modulating cell surface expression of both channels. May also regulate the intracellular trafficking of the ADR1B receptor. May play a role in autophagy. Overexpression results in CFTR intracellular retention and degradation in the lysosomes.<ref>PMID:11707463</ref> <ref>PMID:14570915</ref> <ref>PMID:15358775</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			PDZ (PSD-95/Dlg/ZO-1) binding domains often serve as cellular traffic engineers, controlling the localization and activity of a wide variety of binding partners. As a result, they play important roles in both physiological and pathological processes. However, PDZ binding specificities overlap, allowing multiple PDZ proteins to mediate distinct effects on shared binding partners. For example, several PDZ domains bind the cystic fibrosis (CF) transmembrane conductance regulator (CFTR), an epithelial ion channel mutated in CF. Among these binding partners, the CFTR-associated ligand (CAL) facilitates post-maturational degradation of the channel and is thus a potential therapeutic target. Using iterative optimization, we previously developed a selective CAL inhibitor peptide (iCAL36). Here, we investigate the stereochemical basis of iCAL36 specificity. The crystal structure of iCAL36 in complex with the CAL PDZ domain reveals stereochemical interactions distributed along the peptide-binding cleft, despite the apparent degeneracy of the CAL binding motif. A critical selectivity determinant that distinguishes CAL from other CFTR-binding PDZ domains is the accommodation of an isoleucine residue at the C-terminal position (P(0)), a characteristic shared with the Tax-interacting protein-1. Comparison of the structures of these two PDZ domains in complex with ligands containing P(0) Leu or Ile residues reveals two distinct modes of accommodation for beta-branched C-terminal side chains. Access to each mode is controlled by distinct residues in the carboxylate-binding loop. These studies provide new insights into the primary sequence determinants of binding motifs, which in turn control the scope and evolution of PDZ interactomes.

	~~==Disease==~~		Stereochemical Determinants of C-terminal Specificity in PDZ Peptide-binding Domains: A NOVEL CONTRIBUTION OF THE CARBOXYLATE-BINDING LOOP.,Amacher JF, Cushing PR, Bahl CD, Beck T, Madden DR J Biol Chem. 2013 Feb 15;288(7):5114-26. doi: 10.1074/jbc.M112.401588. Epub 2012 , Dec 15. PMID:23243314<ref>PMID:23243314</ref>
	~~[[http~~:~~//www~~.~~uniprot~~.~~org/uniprot/GOPC_HUMAN GOPC_HUMAN]] Note=A chromosomal aberration involving GOPC is found in a glioblastoma multiforme sample. An intra-chromosomal deletion del~~(6)~~(q21q21) is responsible for the formation of GOPC~~-~~ROS1 chimeric protein which has a constitutive receptor tyrosine kinase activity~~.<ref>PMID:~~12661006~~</ref>

	~~==Function==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[http:/~~/~~www.uniprot.org/uniprot/GOPC_HUMAN GOPC_HUMAN]] Plays~~ a ~~role in intracellular protein trafficking and degradation. May regulate CFTR chloride currents and acid-induced ASIC3 currents by modulating cell surface expression~~ of ~~both channels. May also regulate~~ the ~~intracellular trafficking of the ADR1B receptor~~. ~~May play a role in autophagy~~. ~~Overexpression results in CFTR intracellular retention and degradation in the lysosomes~~.<~~ref~~>~~PMID:11707463</ref><ref>PMID:14570915~~</~~ref><ref>PMID:15358775</ref~~>		</div>
			== References ==
	==~~About this Structure==~~		<references/>
	[[4e35]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E35 OCA].		__TOC__
			</StructureSection>
	~~==Reference~~==
	<references ~~group="xtra"~~/><~~references~~/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Amacher, J F.]]		[[Category: Amacher, J F]]
	[[Category: Madden, D R.]]		[[Category: Madden, D R]]
	[[Category: Pdz-peptide complex]]		[[Category: Pdz-peptide complex]]
	[[Category: Protein transport-protein binding complex]]		[[Category: Protein transport-protein binding complex]]

OCA at 06:17, 25 March 2013

2013-03-25T06:17:09Z

← Older revision		Revision as of 06:17, 25 March 2013
Line 1:		Line 1:
	~~[[Image:4e35.png\|left\|200px]]~~

	{{STRUCTURE_4e35\| PDB=4e35 \| SCENE= }}		{{STRUCTURE_4e35\| PDB=4e35 \| SCENE= }}
			===Crystal structure of CFTR Associated Ligand (CAL) PDZ domain bound to iCAL36-L (ANSRWPTSIL) peptide===
			{{ABSTRACT_PUBMED_23243314}}

	===~~Crystal structure of CFTR Associated Ligand~~ (~~CAL~~) ~~PDZ domain bound to iCAL36-L~~ (~~ANSRWPTSIL~~) ~~peptide===~~		==Disease==
			[[http://www.uniprot.org/uniprot/GOPC_HUMAN GOPC_HUMAN]] Note=A chromosomal aberration involving GOPC is found in a glioblastoma multiforme sample. An intra-chromosomal deletion del(6)(q21q21) is responsible for the formation of GOPC-ROS1 chimeric protein which has a constitutive receptor tyrosine kinase activity.<ref>PMID:12661006</ref>

	~~{{ABSTRACT_PUBMED_23243314}}~~		==Function==
			[[http://www.uniprot.org/uniprot/GOPC_HUMAN GOPC_HUMAN]] Plays a role in intracellular protein trafficking and degradation. May regulate CFTR chloride currents and acid-induced ASIC3 currents by modulating cell surface expression of both channels. May also regulate the intracellular trafficking of the ADR1B receptor. May play a role in autophagy. Overexpression results in CFTR intracellular retention and degradation in the lysosomes.<ref>PMID:11707463</ref><ref>PMID:14570915</ref><ref>PMID:15358775</ref>

	==About this Structure==		==About this Structure==
	[[4e35]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E35 OCA].		[[4e35]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E35 OCA].

			==Reference==
			<references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Amacher, J F.]]		[[Category: Amacher, J F.]]

OCA at 13:20, 6 March 2013

2013-03-06T13:20:03Z

← Older revision		Revision as of 13:20, 6 March 2013
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	~~'''Unreleased structure'''~~		[[Image:4e35.png\|left\|200px]]

	~~The entry~~ 4e35 ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_4e35\| PDB=4e35 \| SCENE= }}

	~~Authors: Amacher, J.F., Madden, D.R.~~		===Crystal structure of CFTR Associated Ligand (CAL) PDZ domain bound to iCAL36-L (ANSRWPTSIL) peptide===

	~~Description~~: ~~Crystal structure of CFTR Associated Ligand (CAL) PDZ domain bound to iCAL36~~-~~L (ANSRWPTSIL)~~ peptide		{{ABSTRACT_PUBMED_23243314}}

			==About this Structure==
			[[4e35]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E35 OCA].
			[[Category: Homo sapiens]]
			[[Category: Amacher, J F.]]
			[[Category: Madden, D R.]]
			[[Category: Pdz-peptide complex]]
			[[Category: Protein transport-protein binding complex]]

OCA at 05:24, 30 May 2012

2012-05-30T05:24:20Z

← Older revision		Revision as of 05:24, 30 May 2012
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	Authors: Amacher, J.F., Madden, D.R.		Authors: Amacher, J.F., Madden, D.R.

	Description: Crystal structure of CFTR Associated Ligand (CAL) PDZ domain bound to ~~iCAL50~~ (ANSRWPTSIL) peptide		Description: Crystal structure of CFTR Associated Ligand (CAL) PDZ domain bound to iCAL36-L (ANSRWPTSIL) peptide

OCA at 05:35, 23 May 2012

2012-05-23T05:35:22Z

← Older revision		Revision as of 05:35, 23 May 2012
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4e35 is ON HOLD		The entry 4e35 is ON HOLD until Paper Publication

	Authors: Amacher, J.F., Madden, D.R.		Authors: Amacher, J.F., Madden, D.R.

	Description: Crystal structure of CFTR Associated Ligand (CAL) PDZ domain bound to iCAL50 (ANSRWPTSIL) peptide		Description: Crystal structure of CFTR Associated Ligand (CAL) PDZ domain bound to iCAL50 (ANSRWPTSIL) peptide

OCA: Protected "4e35" [edit=sysop:move=sysop]

2012-03-21T07:15:30Z

Protected "4e35" [edit=sysop:move=sysop]

← Older revision	Revision as of 07:15, 21 March 2012
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4e35 is ON HOLD Authors: Amacher, J.F., Madden, D.R. Description: Crystal structure of CFTR Associated Ligand (CAL) PDZ domain bound to iCAL50 (ANS...

2012-03-21T07:15:29Z

New page: '''Unreleased structure''' The entry 4e35 is ON HOLD Authors: Amacher, J.F., Madden, D.R. Description: Crystal structure of CFTR Associated Ligand (CAL) PDZ domain bound to iCAL50 (ANS...

New page

'''Unreleased structure'''

The entry 4e35 is ON HOLD

Authors: Amacher, J.F., Madden, D.R.

Description: Crystal structure of CFTR Associated Ligand (CAL) PDZ domain bound to iCAL50 (ANSRWPTSIL) peptide