6k3f - Revision history

OCA at 10:26, 22 November 2023

2023-11-22T10:26:14Z

←Older revision		Revision as of 10:26, 22 November 2023
Line 3:		Line 3:
	<StructureSection load='6k3f' size='340' side='right'caption='[[6k3f]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='6k3f' size='340' side='right'caption='[[6k3f]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6k3f]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K3F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K3F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6k3f]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=6K3F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K3F FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=SEP:PHOSPHOSERINE'>SEP</scene~~>, ~~<scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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]] 2.3Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~Arrb2 ([https~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=10116 Buffalo rat])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=6k3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k3f OCA], [https://pdbe.org/6k3f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k3f RCSB], [https://www.ebi.ac.uk/pdbsum/6k3f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k3f 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=6k3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k3f OCA], [https://pdbe.org/6k3f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k3f RCSB], [https://www.ebi.ac.uk/pdbsum/6k3f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k3f ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ARRB2_RAT ARRB2_RAT]] Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Mediates endocytosis of CCR7 following ligation of CCL19 but not CCL21. Involved in internalization of P2RY1, P2RY4, P2RY6 and P2RY11 and ATP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 and subsequent recycling or degradation. Involved in ubiquitination of IGF1R. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2) and MAPK10 (JNK3). ERK1/2 and JNK3 activated by the beta-arrestin scaffold are largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Acts as signaling scaffold for the AKT1 pathway. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Increases ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Involved in CCR7-mediated ERK1/2 signaling involving ligand CCL19. Is involved in type-1A angiotensin II receptor/AGTR1-mediated ERK activity. Is involved in type-1A angiotensin II receptor/AGTR1-mediated MAPK10 activity. Is involved in dopamine-stimulated AKT1 activity in the striatum by disrupting the association of AKT1 with its negative regulator PP2A. Involved in AGTR1-mediated chemotaxis. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. Suppresses UV-induced NF-kappa-B-dependent activation by interacting with CHUK. The function is promoted by stimulation of ADRB2 and dephosphorylation of ARRB2. Involved in IL8-mediated granule release in neutrophils (By similarity). Involved in p53/TP53-mediated apoptosis by regulating MDM2 and reducing the MDM2-mediated degradation of p53/TP53. May serve as nuclear messenger for GPCRs. Upon stimulation of OR1D2, may be involved in regulation of gene expression during the early processes of fertilization. Also involved in regulation of receptors other than GPCRs. Involved in endocytosis of TGFBR2 and TGFBR3 and down-regulates TGF-beta signaling such as NF-kappa-B activation. Involved in endocytosis of low-density lipoprotein receptor/LDLR. Involved in endocytosis of smoothened homolog/Smo, which also requires GRK2. Involved in endocytosis of SLC9A5. Involved in endocytosis of ENG and subsequent TGF-beta-mediated ERK activation and migration of epithelial cells. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Involved in insulin resistance by acting as insulin-induced signaling scaffold for SRC, AKT1 and INSR. Involved in regulation of inhibitory signaling of natural killer cells by recruiting PTPN6 and PTPN11 to KIR2DL1. Involved in the internalization of the atypical chemokine receptor ACKR3 (By similarity). Acts as an adapter protein coupling FFAR4 receptor to specific downstream signaling pathways, as well as mediating receptor endocytosis. During the activation step of NLRP3 inflammasome, directly associates with NLRP3 leading to inhibition of proinflammatory cytokine release and inhibition of inflammation.[UniProtKB:P32121]<ref>PMID:10097102</ref> <ref>PMID:10747877</ref> <ref>PMID:11090355</ref> <ref>PMID:11226259</ref> <ref>PMID:11777902</ref> <ref>PMID:12464600</ref> <ref>PMID:15878855</ref> <ref>PMID:18006496</ref> <ref>PMID:18408005</ref> <ref>PMID:19055777</ref> [[https://www.uniprot.org/uniprot/ACKR3_HUMAN ACKR3_HUMAN]] Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.<ref>PMID:16107333</ref> <ref>PMID:16940167</ref> <ref>PMID:17804806</ref> <ref>PMID:18653785</ref> <ref>PMID:19255243</ref> <ref>PMID:19380869</ref> <ref>PMID:19641136</ref> <ref>PMID:20018651</ref> <ref>PMID:20161793</ref> <ref>PMID:20388803</ref> <ref>PMID:20887389</ref> <ref>PMID:22300987</ref>	+	[https://www.uniprot.org/uniprot/ARRB2_RAT ARRB2_RAT] Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Mediates endocytosis of CCR7 following ligation of CCL19 but not CCL21. Involved in internalization of P2RY1, P2RY4, P2RY6 and P2RY11 and ATP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 and subsequent recycling or degradation. Involved in ubiquitination of IGF1R. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2) and MAPK10 (JNK3). ERK1/2 and JNK3 activated by the beta-arrestin scaffold are largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Acts as signaling scaffold for the AKT1 pathway. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Increases ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Involved in CCR7-mediated ERK1/2 signaling involving ligand CCL19. Is involved in type-1A angiotensin II receptor/AGTR1-mediated ERK activity. Is involved in type-1A angiotensin II receptor/AGTR1-mediated MAPK10 activity. Is involved in dopamine-stimulated AKT1 activity in the striatum by disrupting the association of AKT1 with its negative regulator PP2A. Involved in AGTR1-mediated chemotaxis. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. Suppresses UV-induced NF-kappa-B-dependent activation by interacting with CHUK. The function is promoted by stimulation of ADRB2 and dephosphorylation of ARRB2. Involved in IL8-mediated granule release in neutrophils (By similarity). Involved in p53/TP53-mediated apoptosis by regulating MDM2 and reducing the MDM2-mediated degradation of p53/TP53. May serve as nuclear messenger for GPCRs. Upon stimulation of OR1D2, may be involved in regulation of gene expression during the early processes of fertilization. Also involved in regulation of receptors other than GPCRs. Involved in endocytosis of TGFBR2 and TGFBR3 and down-regulates TGF-beta signaling such as NF-kappa-B activation. Involved in endocytosis of low-density lipoprotein receptor/LDLR. Involved in endocytosis of smoothened homolog/Smo, which also requires GRK2. Involved in endocytosis of SLC9A5. Involved in endocytosis of ENG and subsequent TGF-beta-mediated ERK activation and migration of epithelial cells. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Involved in insulin resistance by acting as insulin-induced signaling scaffold for SRC, AKT1 and INSR. Involved in regulation of inhibitory signaling of natural killer cells by recruiting PTPN6 and PTPN11 to KIR2DL1. Involved in the internalization of the atypical chemokine receptor ACKR3 (By similarity). Acts as an adapter protein coupling FFAR4 receptor to specific downstream signaling pathways, as well as mediating receptor endocytosis. During the activation step of NLRP3 inflammasome, directly associates with NLRP3 leading to inhibition of proinflammatory cytokine release and inhibition of inflammation.[UniProtKB:P32121]<ref>PMID:10097102</ref> <ref>PMID:10747877</ref> <ref>PMID:11090355</ref> <ref>PMID:11226259</ref> <ref>PMID:11777902</ref> <ref>PMID:12464600</ref> <ref>PMID:15878855</ref> <ref>PMID:18006496</ref> <ref>PMID:18408005</ref> <ref>PMID:19055777</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Buffalo rat~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lee, H H~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: ~~Min, K J~~]]	+	[[Category: Lee HH]]
-	[[Category: ~~Yoon, H J~~]]	+	[[Category: Min KJ]]
-	[[Category: ~~Complex]]~~	+	[[Category: Yoon HJ]]
-	~~[[Category: Signaling protein~~]]	+

OCA at 07:40, 25 June 2021

2021-06-25T07:40:40Z

←Older revision		Revision as of 07:40, 25 June 2021
Line 1:		Line 1:

-	==Crystal ~~structure~~ of ~~a cell signaling protein~~ in ~~complex~~ with ~~chemokine-related protein 1~~==	+	==Crystal Structure of beta-Arrestin 2 in Complex with CXCR7 Phosphopeptide==
-	<StructureSection load='6k3f' size='340' side='right'caption='[[6k3f]]' scene=''>	+	<StructureSection load='6k3f' size='340' side='right'caption='[[6k3f]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K3F OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6K3F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6k3f]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K3F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K3F FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6k3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k3f OCA], [~~http~~://pdbe.org/6k3f PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6k3f RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6k3f PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6k3f ProSAT]</span></td></tr>	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Arrb2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=6k3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k3f OCA], [https://pdbe.org/6k3f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k3f RCSB], [https://www.ebi.ac.uk/pdbsum/6k3f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k3f ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/ARRB2_RAT ARRB2_RAT]] Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Mediates endocytosis of CCR7 following ligation of CCL19 but not CCL21. Involved in internalization of P2RY1, P2RY4, P2RY6 and P2RY11 and ATP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 and subsequent recycling or degradation. Involved in ubiquitination of IGF1R. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2) and MAPK10 (JNK3). ERK1/2 and JNK3 activated by the beta-arrestin scaffold are largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Acts as signaling scaffold for the AKT1 pathway. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Increases ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Involved in CCR7-mediated ERK1/2 signaling involving ligand CCL19. Is involved in type-1A angiotensin II receptor/AGTR1-mediated ERK activity. Is involved in type-1A angiotensin II receptor/AGTR1-mediated MAPK10 activity. Is involved in dopamine-stimulated AKT1 activity in the striatum by disrupting the association of AKT1 with its negative regulator PP2A. Involved in AGTR1-mediated chemotaxis. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. Suppresses UV-induced NF-kappa-B-dependent activation by interacting with CHUK. The function is promoted by stimulation of ADRB2 and dephosphorylation of ARRB2. Involved in IL8-mediated granule release in neutrophils (By similarity). Involved in p53/TP53-mediated apoptosis by regulating MDM2 and reducing the MDM2-mediated degradation of p53/TP53. May serve as nuclear messenger for GPCRs. Upon stimulation of OR1D2, may be involved in regulation of gene expression during the early processes of fertilization. Also involved in regulation of receptors other than GPCRs. Involved in endocytosis of TGFBR2 and TGFBR3 and down-regulates TGF-beta signaling such as NF-kappa-B activation. Involved in endocytosis of low-density lipoprotein receptor/LDLR. Involved in endocytosis of smoothened homolog/Smo, which also requires GRK2. Involved in endocytosis of SLC9A5. Involved in endocytosis of ENG and subsequent TGF-beta-mediated ERK activation and migration of epithelial cells. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Involved in insulin resistance by acting as insulin-induced signaling scaffold for SRC, AKT1 and INSR. Involved in regulation of inhibitory signaling of natural killer cells by recruiting PTPN6 and PTPN11 to KIR2DL1. Involved in the internalization of the atypical chemokine receptor ACKR3 (By similarity). Acts as an adapter protein coupling FFAR4 receptor to specific downstream signaling pathways, as well as mediating receptor endocytosis. During the activation step of NLRP3 inflammasome, directly associates with NLRP3 leading to inhibition of proinflammatory cytokine release and inhibition of inflammation.[UniProtKB:P32121]<ref>PMID:10097102</ref> <ref>PMID:10747877</ref> <ref>PMID:11090355</ref> <ref>PMID:11226259</ref> <ref>PMID:11777902</ref> <ref>PMID:12464600</ref> <ref>PMID:15878855</ref> <ref>PMID:18006496</ref> <ref>PMID:18408005</ref> <ref>PMID:19055777</ref> [[https://www.uniprot.org/uniprot/ACKR3_HUMAN ACKR3_HUMAN]] Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.<ref>PMID:16107333</ref> <ref>PMID:16940167</ref> <ref>PMID:17804806</ref> <ref>PMID:18653785</ref> <ref>PMID:19255243</ref> <ref>PMID:19380869</ref> <ref>PMID:19641136</ref> <ref>PMID:20018651</ref> <ref>PMID:20161793</ref> <ref>PMID:20388803</ref> <ref>PMID:20887389</ref> <ref>PMID:22300987</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	beta-Arrestins (betaarrs) critically regulate G-protein-coupled receptor (GPCR) signaling and trafficking. betaarrs have two isoforms, betaarr1 and betaarr2. Receptor phosphorylation is a key determinant for the binding of betaarrs, and understanding the intricate details of receptor-betaarr interaction is the next frontier in GPCR structural biology. The high-resolution structure of active betaarr1 in complex with a phosphopeptide derived from GPCR has been revealed, but that of betaarr2 remains elusive. Here, we present a 2.3-A crystal structure of betaarr2 in complex with a phosphopeptide (C7pp) derived from the carboxyl terminus of CXCR7. The structural analysis of C7pp-bound betaarr2 reveals key differences from the previously determined active conformation of betaarr1. One of the key differences is that C7pp-bound betaarr2 shows a relatively small inter-domain rotation. Antibody-fragment-based conformational sensor and hydrogen/deuterium exchange experiments further corroborated the structural features of betaarr2 and suggested that betaarr2 adopts a range of inter-domain rotations.
		+
		+	Crystal Structure of beta-Arrestin 2 in Complex with CXCR7 Phosphopeptide.,Min K, Yoon HJ, Park JY, Baidya M, Dwivedi-Agnihotri H, Maharana J, Chaturvedi M, Chung KY, Shukla AK, Lee HH Structure. 2020 Sep 1;28(9):1014-1023.e4. doi: 10.1016/j.str.2020.06.002. Epub, 2020 Jun 23. PMID:32579945<ref>PMID:32579945</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6k3f" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Arrestin 3D structures\|Arrestin 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Buffalo rat]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Lee HH]]	+	[[Category: Lee, H H]]
-	[[Category: Min KJ]]	+	[[Category: Min, K J]]
-	[[Category: Yoon HJ]]	+	[[Category: Yoon, H J]]
		+	[[Category: Complex]]
		+	[[Category: Signaling protein]]

OCA at 06:22, 10 June 2020

2020-06-10T06:22:14Z

←Older revision		Revision as of 06:22, 10 June 2020
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-	'''Unreleased structure'''

-	~~The entry~~ 6k3f ~~is ON HOLD until Paper Publication~~	+	==Crystal structure of a cell signaling protein in complex with chemokine-related protein 1==
-		+	<StructureSection load='6k3f' size='340' side='right'caption='[[6k3f]]' scene=''>
-	~~Authors~~: ~~Min~~, K.J., ~~Yoon~~, H.J., ~~Lee~~, H.H.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K3F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6K3F FirstGlance]. <br>
-	~~Description: Crystal structure of a cell signaling protein in complex with chemokine-related protein 1~~	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6k3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k3f OCA], [http://pdbe.org/6k3f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k3f RCSB], [http://www.ebi.ac.uk/pdbsum/6k3f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k3f ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: ~~Min, K.J~~]]	+	__TOC__
-	[[Category: ~~Lee, H.H~~]]	+	</StructureSection>
-	[[Category: Yoon~~, H.J~~]]	+	[[Category: Large Structures]]
		+	[[Category: Lee HH]]
		+	[[Category: Min KJ]]
		+	[[Category: Yoon HJ]]

OCA at 05:05, 3 June 2020

2020-06-03T05:05:09Z

←Older revision		Revision as of 05:05, 3 June 2020
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6k3f is ON HOLD until ~~Aug 18 2021~~	+	The entry 6k3f is ON HOLD until Paper Publication

	Authors: Min, K.J., Yoon, H.J., Lee, H.H.		Authors: Min, K.J., Yoon, H.J., Lee, H.H.
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	Description: Crystal structure of a cell signaling protein in complex with chemokine-related protein 1		Description: Crystal structure of a cell signaling protein in complex with chemokine-related protein 1
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Lee, H.H]]
	[[Category: Min, K.J]]		[[Category: Min, K.J]]
		+	[[Category: Lee, H.H]]
	[[Category: Yoon, H.J]]		[[Category: Yoon, H.J]]

OCA at 03:46, 13 May 2020

2020-05-13T03:46:46Z

←Older revision		Revision as of 03:46, 13 May 2020
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6k3f is ON HOLD until ~~Paper Publication~~	+	The entry 6k3f is ON HOLD until Aug 18 2021

	Authors: Min, K.J., Yoon, H.J., Lee, H.H.		Authors: Min, K.J., Yoon, H.J., Lee, H.H.

OCA at 04:56, 6 November 2019

2019-11-06T04:56:34Z

←Older revision		Revision as of 04:56, 6 November 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6k3f is ON HOLD	+	The entry 6k3f is ON HOLD until Paper Publication

	Authors: Min, K.J., Yoon, H.J., Lee, H.H.		Authors: Min, K.J., Yoon, H.J., Lee, H.H.

OCA at 07:14, 30 October 2019

2019-10-30T07:14:38Z

←Older revision		Revision as of 07:14, 30 October 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6k3f is ON HOLD ~~until Paper Publication~~	+	The entry 6k3f is ON HOLD

	Authors: Min, K.J., Yoon, H.J., Lee, H.H.		Authors: Min, K.J., Yoon, H.J., Lee, H.H.
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	Description: Crystal structure of a cell signaling protein in complex with chemokine-related protein 1		Description: Crystal structure of a cell signaling protein in complex with chemokine-related protein 1
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Min, K.J]]
	[[Category: Lee, H.H]]		[[Category: Lee, H.H]]
		+	[[Category: Min, K.J]]
	[[Category: Yoon, H.J]]		[[Category: Yoon, H.J]]

OCA at 06:30, 2 October 2019

2019-10-02T06:30:13Z

←Older revision		Revision as of 06:30, 2 October 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6k3f is ON HOLD	+	The entry 6k3f is ON HOLD until Paper Publication

	Authors: Min, K.J., Yoon, H.J., Lee, H.H.		Authors: Min, K.J., Yoon, H.J., Lee, H.H.
Line 7:		Line 7:
	Description: Crystal structure of a cell signaling protein in complex with chemokine-related protein 1		Description: Crystal structure of a cell signaling protein in complex with chemokine-related protein 1
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Lee, H.H]]
	[[Category: Min, K.J]]		[[Category: Min, K.J]]
		+	[[Category: Lee, H.H]]
	[[Category: Yoon, H.J]]		[[Category: Yoon, H.J]]

OCA: Protected "6k3f" [edit=sysop:move=sysop]

2019-05-29T04:25:03Z

Protected "6k3f" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:25, 29 May 2019

OCA: New page: '''Unreleased structure''' The entry 6k3f is ON HOLD Authors: Min, K.J., Yoon, H.J., Lee, H.H. Description: Crystal structure of a cell signaling protein in complex with chemokine-rela...

2019-05-29T04:25:01Z

New page: '''Unreleased structure''' The entry 6k3f is ON HOLD Authors: Min, K.J., Yoon, H.J., Lee, H.H. Description: Crystal structure of a cell signaling protein in complex with chemokine-rela...

New page

'''Unreleased structure'''

The entry 6k3f is ON HOLD

Authors: Min, K.J., Yoon, H.J., Lee, H.H.

Description: Crystal structure of a cell signaling protein in complex with chemokine-related protein 1
[[Category: Unreleased Structures]]
[[Category: Lee, H.H]]
[[Category: Min, K.J]]
[[Category: Yoon, H.J]]