4rtv - Revision history

OCA at 17:55, 20 September 2023

OCA — Wed, 20 Sep 2023 17:55:57 GMT

←Older revision		Revision as of 17:55, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4rtv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RTV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RTV FirstGlance]. <br>		<table><tr><td colspan='2'>[[4rtv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RTV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RTV FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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]] 1.37Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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=4rtv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rtv OCA], [https://pdbe.org/4rtv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rtv RCSB], [https://www.ebi.ac.uk/pdbsum/4rtv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rtv 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=4rtv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rtv OCA], [https://pdbe.org/4rtv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rtv RCSB], [https://www.ebi.ac.uk/pdbsum/4rtv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rtv ProSAT]</span></td></tr>
	</table>		</table>

OCA at 08:28, 8 March 2023

OCA — Wed, 08 Mar 2023 08:28:08 GMT

←Older revision		Revision as of 08:28, 8 March 2023
Line 3:		Line 3:
	<StructureSection load='4rtv' size='340' side='right'caption='[[4rtv]], [[Resolution\|resolution]] 1.37Å' scene=''>		<StructureSection load='4rtv' size='340' side='right'caption='[[4rtv]], [[Resolution\|resolution]] 1.37Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4rtv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RTV OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4RTV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4rtv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RTV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RTV FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4rtu\|4rtu]], [[4rtw\|4rtw]], [[4rty\|4rty]], [[4rtz\|4rtz]], [[4rtx\|4rtx]]</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=4rtv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rtv OCA], [https://pdbe.org/4rtv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rtv RCSB], [https://www.ebi.ac.uk/pdbsum/4rtv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rtv ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_protein-tyrosine_kinase Non-specific protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.2 2.7.10.2] </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=4rtv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rtv OCA], [~~http~~://pdbe.org/4rtv PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4rtv RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4rtv PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4rtv ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SRC_CHICK SRC_CHICK]] Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates involved in this process. When cells adhere via focal adhesions to the extra-cellular matrix, signals are transmitted by integrins into the cell and result in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). Also active at the sites of cell-cell contact adherens junctions and at gap junctions. Implicated in the regulation of pre-mRNA-processing. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus.<ref>PMID:1717492</ref> <ref>PMID:8550628</ref>	+	[https://www.uniprot.org/uniprot/SRC_CHICK SRC_CHICK] Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates involved in this process. When cells adhere via focal adhesions to the extra-cellular matrix, signals are transmitted by integrins into the cell and result in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). Also active at the sites of cell-cell contact adherens junctions and at gap junctions. Implicated in the regulation of pre-mRNA-processing. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus.<ref>PMID:1717492</ref> <ref>PMID:8550628</ref>

	==See Also==		==See Also==
-	*[[Tyrosine kinase\|Tyrosine kinase]]	+	*[[Tyrosine kinase 3D structures\|Tyrosine kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Gallus gallus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Non-specific protein-tyrosine kinase~~]]	+	[[Category: Synthetic construct]]
-	[[Category: Bacarizo, J]]	+	[[Category: Bacarizo J]]
-	[[Category: Camara-Artigas, A]]	+	[[Category: Camara-Artigas A]]
-	~~[[Category: Beta shandwich]]~~	+
-	~~[[Category: Protein binding]]~~	+
-	~~[[Category: Sh3 domain]]~~	+
-	~~[[Category: Signaling protein~~]]	+

OCA at 09:14, 21 May 2019

OCA — Tue, 21 May 2019 09:14:52 GMT

←Older revision		Revision as of 09:14, 21 May 2019
Line 1:		Line 1:

	==Crystal structure of the Src tyrosine kinase SH3 domain S94A/Q128R mutant in complex with the high affinity synthetic peptide APP12==		==Crystal structure of the Src tyrosine kinase SH3 domain S94A/Q128R mutant in complex with the high affinity synthetic peptide APP12==
-	<StructureSection load='4rtv' size='340' side='right' caption='[[4rtv]], [[Resolution\|resolution]] 1.37Å' scene=''>	+	<StructureSection load='4rtv' size='340' side='right'caption='[[4rtv]], [[Resolution\|resolution]] 1.37Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4rtv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RTV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RTV FirstGlance]. <br>		<table><tr><td colspan='2'>[[4rtv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RTV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RTV FirstGlance]. <br>
Line 18:		Line 18:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Non-specific protein-tyrosine kinase]]		[[Category: Non-specific protein-tyrosine kinase]]
	[[Category: Bacarizo, J]]		[[Category: Bacarizo, J]]

OCA at 16:46, 18 August 2017

OCA — Fri, 18 Aug 2017 16:46:10 GMT

←Older revision		Revision as of 16:46, 18 August 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 4rtv is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Crystal structure of the Src tyrosine kinase SH3 domain S94A/Q128R mutant in complex with the high affinity synthetic peptide APP12==
		+	<StructureSection load='4rtv' size='340' side='right' caption='[[4rtv]], [[Resolution\|resolution]] 1.37Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4rtv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RTV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RTV FirstGlance]. <br>
		+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4rtu\|4rtu]], [[4rtw\|4rtw]], [[4rty\|4rty]], [[4rtz\|4rtz]], [[4rtx\|4rtx]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_protein-tyrosine_kinase Non-specific protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.2 2.7.10.2] </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=4rtv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rtv OCA], [http://pdbe.org/4rtv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rtv RCSB], [http://www.ebi.ac.uk/pdbsum/4rtv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rtv ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SRC_CHICK SRC_CHICK]] Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates involved in this process. When cells adhere via focal adhesions to the extra-cellular matrix, signals are transmitted by integrins into the cell and result in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). Also active at the sites of cell-cell contact adherens junctions and at gap junctions. Implicated in the regulation of pre-mRNA-processing. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus.<ref>PMID:1717492</ref> <ref>PMID:8550628</ref>

-	~~Authors: Camara-Artigas, A., Bacarizo, J.~~	+	==See Also==
-		+	*[[Tyrosine kinase\|Tyrosine kinase]]
-	~~Description: Crystal structure of the Src tyrosine~~ kinase ~~SH3 domain S94A~~/~~Q128R mutant in complex with the high affinity synthetic peptide APP12~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Non-specific protein-tyrosine kinase]]
	[[Category: Bacarizo, J]]		[[Category: Bacarizo, J]]
	[[Category: Camara-Artigas, A]]		[[Category: Camara-Artigas, A]]
		+	[[Category: Beta shandwich]]
		+	[[Category: Protein binding]]
		+	[[Category: Sh3 domain]]
		+	[[Category: Signaling protein]]

OCA at 17:21, 24 December 2014

OCA — Wed, 24 Dec 2014 17:21:50 GMT

←Older revision		Revision as of 17:21, 24 December 2014
Line 6:		Line 6:

	Description: Crystal structure of the Src tyrosine kinase SH3 domain S94A/Q128R mutant in complex with the high affinity synthetic peptide APP12		Description: Crystal structure of the Src tyrosine kinase SH3 domain S94A/Q128R mutant in complex with the high affinity synthetic peptide APP12
		+	[[Category: Unreleased Structures]]
		+	[[Category: Bacarizo, J]]
		+	[[Category: Camara-Artigas, A]]

OCA at 11:06, 17 December 2014

OCA — Wed, 17 Dec 2014 11:06:19 GMT

←Older revision		Revision as of 11:06, 17 December 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Camara-Artigas, A., Bacarizo, J.		Authors: Camara-Artigas, A., Bacarizo, J.

	Description: Crystal structure of the Src tyrosine kinase SH3 domain S94A/Q128R mutant in complex with the high affinity synthetic peptide APP12		Description: Crystal structure of the Src tyrosine kinase SH3 domain S94A/Q128R mutant in complex with the high affinity synthetic peptide APP12

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

OCA — Wed, 26 Nov 2014 06:47:26 GMT

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

←Older revision

Revision as of 06:47, 26 November 2014

OCA: New page: '''Unreleased structure''' The entry 4rtv is ON HOLD Authors: Camara-Artigas, A., Bacarizo, J. Description: Crystal structure of the Src tyrosine kinase SH3 domain S94A/Q128R mutant in...

OCA — Wed, 26 Nov 2014 06:47:25 GMT

New page: '''Unreleased structure''' The entry 4rtv is ON HOLD Authors: Camara-Artigas, A., Bacarizo, J. Description: Crystal structure of the Src tyrosine kinase SH3 domain S94A/Q128R mutant in...

New page

'''Unreleased structure'''

The entry 4rtv is ON HOLD

Authors: Camara-Artigas, A., Bacarizo, J.

Description: Crystal structure of the Src tyrosine kinase SH3 domain S94A/Q128R mutant in complex with the high affinity synthetic peptide APP12