6bd2 - Revision history

OCA at 14:38, 4 October 2023

2023-10-04T14:38:32Z

← Older revision		Revision as of 14:38, 4 October 2023
Line 3:		Line 3:
	<StructureSection load='6bd2' size='340' side='right'caption='[[6bd2]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='6bd2' size='340' side='right'caption='[[6bd2]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6bd2]] is a 3 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=6BD2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6BD2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[6bd2]] is a 3 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=6BD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BD2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 2.9Å</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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <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">YWHAQ ([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'>[https://proteopedia.org/fgij/fg.htm?mol=6bd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bd2 OCA], [https://pdbe.org/6bd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bd2 RCSB], [https://www.ebi.ac.uk/pdbsum/6bd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bd2 ProSAT]</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=6bd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bd2 OCA], [~~http~~://pdbe.org/6bd2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6bd2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6bd2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6bd2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/1433T_HUMAN 1433T_HUMAN]] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1.<ref>PMID:12177059</ref> [[http://www.uniprot.org/uniprot/BAIP2_HUMAN BAIP2_HUMAN]] Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection.<ref>PMID:11130076</ref> <ref>PMID:11696321</ref> <ref>PMID:14752106</ref> <ref>PMID:19366662</ref>		[https://www.uniprot.org/uniprot/1433T_HUMAN 1433T_HUMAN] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1.<ref>PMID:12177059</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Dominguez, R]]		[[Category: Dominguez R]]
	[[Category: Kast~~, D J]]~~		[[Category: Kast DJ]]
	~~[[Category: Cell motility]]~~
	~~[[Category: Cytoskeleton regulation]]~~
	~~[[Category: Phosphate binding protein]]~~
	~~[[Category: Protein complex]]~~
	~~[[Category: Signaling protein~~]]

OCA at 13:21, 10 May 2019

2019-05-10T13:21:29Z

← Older revision		Revision as of 13:21, 10 May 2019
Line 1:		Line 1:

	==Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and S366==		==Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and S366==
	<StructureSection load='6bd2' size='340' side='right' caption='[[6bd2]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='6bd2' size='340' side='right'caption='[[6bd2]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6bd2]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BD2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BD2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[6bd2]] is a 3 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=6BD2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BD2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></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='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">YWHAQ ([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=6bd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bd2 OCA], [http://pdbe.org/6bd2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bd2 RCSB], [http://www.ebi.ac.uk/pdbsum/6bd2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bd2 ProSAT]</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=6bd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bd2 OCA], [http://pdbe.org/6bd2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bd2 RCSB], [http://www.ebi.ac.uk/pdbsum/6bd2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bd2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/1433T_HUMAN 1433T_HUMAN]] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1.<ref>PMID:12177059</ref> [[http://www.uniprot.org/uniprot/BAIP2_HUMAN BAIP2_HUMAN]] Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection.<ref>PMID:11130076</ref> <ref>PMID:11696321</ref> <ref>PMID:14752106</ref> <ref>PMID:19366662</ref>		[[http://www.uniprot.org/uniprot/1433T_HUMAN 1433T_HUMAN]] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1.<ref>PMID:12177059</ref> [[http://www.uniprot.org/uniprot/BAIP2_HUMAN BAIP2_HUMAN]] Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection.<ref>PMID:11130076</ref> <ref>PMID:11696321</ref> <ref>PMID:14752106</ref> <ref>PMID:19366662</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Filopodia are precursors of dendritic spines and polarized cell migration. The I-BAR-domain protein IRSp53 is a key regulator of filopodia dynamics that couples Rho-GTPase signaling to cytoskeleton and membrane remodeling, playing essential roles in neuronal development and cell motility. Here, we describe the structural-functional basis for 14-3-3-dependent inhibition of IRSp53. Phosphoproteomics, quantitative binding and crystallographic studies demonstrate that 14-3-3 binds to two pairs of phosphorylation sites in IRSp53. Using bicistronic expression, we obtain an IRSp53 heterodimer in which only one subunit is phosphorylated, and show that each subunit of IRSp53 independently binds one 14-3-3 dimer. A FRET-sensor assay using natively phosphorylated IRSp53 reveals opposite conformational changes upon binding of activatory (Cdc42, Eps8) or inhibitory (14-3-3) inputs. Finally, we show that 14-3-3 inhibits IRSp53 binding to membranes. Collectively, our findings support a mechanism whereby phosphorylation-dependent inhibition of IRSp53 by 14-3-3 counters membrane binding and interactions with Cdc42 and downstream cytoskeletal effectors.

			Mechanism of IRSp53 inhibition by 14-3-3.,Kast DJ, Dominguez R Nat Commun. 2019 Jan 29;10(1):483. doi: 10.1038/s41467-019-08317-8. PMID:30696821<ref>PMID:30696821</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 6bd2" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[14-3-3 protein 3D structures\|14-3-3 protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Dominguez, R]]		[[Category: Dominguez, R]]
	[[Category: Kast, D J]]		[[Category: Kast, D J]]

OCA at 05:51, 24 October 2018

2018-10-24T05:51:07Z

← Older revision		Revision as of 05:51, 24 October 2018
Line 1:		Line 1:
	~~'''Unreleased structure'''~~

	~~The entry 6bd2 is ON HOLD until Paper Publication~~		==Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and S366==
			<StructureSection load='6bd2' size='340' side='right' caption='[[6bd2]], [[Resolution\|resolution]] 2.90Å' scene=''>
	~~Authors: Kast, D.J., Dominguez, R.~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[6bd2]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BD2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BD2 FirstGlance]. <br>
	~~Description:~~ Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and S366		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
	[[~~Category~~: ~~Unreleased Structures~~]]		<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>
	[[~~Category~~: ~~Kast~~, D.J]]		<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=6bd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bd2 OCA], [http://pdbe.org/6bd2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bd2 RCSB], [http://www.ebi.ac.uk/pdbsum/6bd2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bd2 ProSAT]</span></td></tr>
			</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/1433T_HUMAN 1433T_HUMAN]] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1.<ref>PMID:12177059</ref> [[http://www.uniprot.org/uniprot/BAIP2_HUMAN BAIP2_HUMAN]] Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection.<ref>PMID:11130076</ref> <ref>PMID:11696321</ref> <ref>PMID:14752106</ref> <ref>PMID:19366662</ref>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
	[[Category: Dominguez, R]]		[[Category: Dominguez, R]]
			[[Category: Kast, D J]]
			[[Category: Cell motility]]
			[[Category: Cytoskeleton regulation]]
			[[Category: Phosphate binding protein]]
			[[Category: Protein complex]]
			[[Category: Signaling protein]]

OCA at 06:20, 15 November 2017

2017-11-15T06:20:37Z

← Older revision		Revision as of 06:20, 15 November 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 6bd2 is ON HOLD		The entry 6bd2 is ON HOLD until Paper Publication

	Authors: Kast, D.J., Dominguez, R.		Authors: Kast, D.J., Dominguez, R.

OCA: Protected "6bd2" [edit=sysop:move=sysop]

2017-11-01T04:56:05Z

Protected "6bd2" [edit=sysop:move=sysop]

← Older revision	Revision as of 04:56, 1 November 2017
(No difference)

OCA: New page: '''Unreleased structure''' The entry 6bd2 is ON HOLD Authors: Kast, D.J., Dominguez, R. Description: Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and S3...

2017-11-01T04:56:04Z

New page: '''Unreleased structure''' The entry 6bd2 is ON HOLD Authors: Kast, D.J., Dominguez, R. Description: Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and S3...

New page

'''Unreleased structure'''

The entry 6bd2 is ON HOLD

Authors: Kast, D.J., Dominguez, R.

Description: Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and S366
[[Category: Unreleased Structures]]
[[Category: Kast, D.J]]
[[Category: Dominguez, R]]