4hvv - Revision history

OCA at 15:11, 20 September 2023

OCA — Wed, 20 Sep 2023 15:11:51 GMT

←Older revision		Revision as of 15:11, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4hvv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HVV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HVV FirstGlance]. <br>		<table><tr><td colspan='2'>[[4hvv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HVV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HVV 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.1Å</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4hvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hvv OCA], [https://pdbe.org/4hvv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hvv RCSB], [https://www.ebi.ac.uk/pdbsum/4hvv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hvv 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=4hvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hvv OCA], [https://pdbe.org/4hvv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hvv RCSB], [https://www.ebi.ac.uk/pdbsum/4hvv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hvv ProSAT]</span></td></tr>
	</table>		</table>

OCA at 08:18, 9 November 2022

OCA — Wed, 09 Nov 2022 08:18:38 GMT

←Older revision		Revision as of 08:18, 9 November 2022
Line 1:		Line 1:

	==Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide APP12==		==Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide APP12==
-	<StructureSection load='4hvv' size='340' side='right' caption='[[4hvv]], [[Resolution\|resolution]] 1.10Å' scene=''>	+	<StructureSection load='4hvv' size='340' side='right'caption='[[4hvv]], [[Resolution\|resolution]] 1.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4hvv]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Chick Chick~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HVV OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4HVV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4hvv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HVV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HVV FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4hvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hvv OCA], [https://pdbe.org/4hvv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hvv RCSB], [https://www.ebi.ac.uk/pdbsum/4hvv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hvv ProSAT]</span></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4hvu\|4hvu]]~~, ~~[[4hvw\|4hvw]], [[1qwe\|1qwe]], [[1qwf\|1qwf]], [[3fj5\|3fj5]], [[1srl\|1srl]]~~<~~/td></tr>~~	+
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b></td><td class="sblockDat">SRC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</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=4hvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hvv OCA], [~~http~~://pdbe.org/4hvv PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4hvv RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4hvv PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4hvv 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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 20:

	==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: ~~Chick~~]]	+	[[Category: Gallus gallus]]
-	[[Category: ~~Non-specific protein-tyrosine kinase~~]]	+	[[Category: Large Structures]]
-	[[Category: Camara-Artigas, A]]	+	[[Category: Camara-Artigas A]]
-	~~[[Category: Beta shandwich]]~~	+
-	~~[[Category: Kinase]]~~	+
-	~~[[Category: Proline rich motif]]~~	+
-	~~[[Category: Sh3 like barrel]]~~	+
-	~~[[Category: Signaling protein-peptide complex~~]]	+

OCA at 08:10, 5 August 2016

OCA — Fri, 05 Aug 2016 08:10:21 GMT

←Older revision		Revision as of 08:10, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide APP12==		==Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide APP12==
	<StructureSection load='4hvv' size='340' side='right' caption='[[4hvv]], [[Resolution\|resolution]] 1.10Å' scene=''>		<StructureSection load='4hvv' size='340' side='right' caption='[[4hvv]], [[Resolution\|resolution]] 1.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4hvv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Gallus_gallus Gallus gallus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HVV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HVV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4hvv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HVV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HVV FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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='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">[[4hvu\|4hvu]], [[4hvw\|4hvw]], [[1qwe\|1qwe]], [[1qwf\|1qwf]], [[3fj5\|3fj5]], [[1srl\|1srl]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4hvu\|4hvu]], [[4hvw\|4hvw]], [[1qwe\|1qwe]], [[1qwf\|1qwf]], [[3fj5\|3fj5]], [[1srl\|1srl]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SRC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 ~~Gallus gallus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SRC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</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='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=4hvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hvv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hvv RCSB], [http://www.ebi.ac.uk/pdbsum/4hvv 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=4hvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hvv OCA], [http://pdbe.org/4hvv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hvv RCSB], [http://www.ebi.ac.uk/pdbsum/4hvv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hvv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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 4hvv" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 27:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Gallus gallus~~]]	+	[[Category: Chick]]
	[[Category: Non-specific protein-tyrosine kinase]]		[[Category: Non-specific protein-tyrosine kinase]]
	[[Category: Camara-Artigas, A]]		[[Category: Camara-Artigas, A]]

OCA at 17:09, 25 December 2014

OCA — Thu, 25 Dec 2014 17:09:54 GMT

←Older revision		Revision as of 17:09, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4hvv\| PDB=4hvv \| SCENE= }}~~	+	==Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide APP12==
-	===Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide APP12===	+	<StructureSection load='4hvv' size='340' side='right' caption='[[4hvv]], [[Resolution\|resolution]] 1.10Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23633584}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4hvv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HVV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HVV FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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">[[4hvu\|4hvu]], [[4hvw\|4hvw]], [[1qwe\|1qwe]], [[1qwf\|1qwf]], [[3fj5\|3fj5]], [[1srl\|1srl]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SRC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])</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=4hvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hvv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hvv RCSB], [http://www.ebi.ac.uk/pdbsum/4hvv PDBsum]</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>		[[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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The atomic resolution crystal structures of complexes between the SH3 domain of the c-Src tyrosine kinase and two high-affinity peptides belonging to class I and class II have been solved. The crystals of the Thr98Asp and Thr98Glu mutants in complex with the APP12 peptide (APPLPPRNRPRL) belonged to the trigonal space group P3121 and in both cases the asymmetric unit was composed of one molecule of the SH3-APP12 complex. The crystals of the Thr98Glu mutant in complex with the VSL12 peptide (VSLARRPLPLP) belonged to the trigonal space group P3221 and the asymmetric unit was also composed of a single molecule of the SH3-VSL12 complex. All crystals were obtained in the presence of PEG 300 under the same conditions as reported for the intertwined dimeric structure of the c-Src SH3 domain, but the presence of the peptide stabilizes the monomeric form of the domain. These structures allow a detailed analysis of the role of salt bridges, cation-pi interactions and hydrogen bonds in the binding of proline-rich motifs to the c-Src SH3 domain. Moreover, these crystallographic structures allow the role of water molecules in the binding of these motifs to the c-Src SH3 domain to be studied for the first time.
		+
		+	Atomic resolution structures of the c-Src SH3 domain in complex with two high-affinity peptides from classes I and II.,Bacarizo J, Camara-Artigas A Acta Crystallogr D Biol Crystallogr. 2013 May;69(Pt 5):756-66. doi:, 10.1107/S0907444913001522. Epub 2013 Apr 11. PMID:23633584<ref>PMID:23633584</ref>

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4hvv]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Gallus_gallus Gallus gallus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4HVV OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:023633584</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Tyrosine kinase\|Tyrosine kinase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Gallus gallus]]		[[Category: Gallus gallus]]
	[[Category: Non-specific protein-tyrosine kinase]]		[[Category: Non-specific protein-tyrosine kinase]]
-	[[Category: Camara-Artigas, A.]]	+	[[Category: Camara-Artigas, A]]
	[[Category: Beta shandwich]]		[[Category: Beta shandwich]]
	[[Category: Kinase]]		[[Category: Kinase]]

OCA at 13:42, 19 June 2013

OCA — Wed, 19 Jun 2013 13:42:01 GMT

←Older revision		Revision as of 13:42, 19 June 2013
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	{{STRUCTURE_4hvv\| PDB=4hvv \| SCENE= }}		{{STRUCTURE_4hvv\| PDB=4hvv \| SCENE= }}
	===Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide APP12===		===Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide APP12===
		+	{{ABSTRACT_PUBMED_23633584}}

	==Function==		==Function==
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	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:023633584</ref><references group="xtra"/><references/>
	[[Category: Gallus gallus]]		[[Category: Gallus gallus]]
	[[Category: Non-specific protein-tyrosine kinase]]		[[Category: Non-specific protein-tyrosine kinase]]

OCA at 07:51, 2 May 2013

OCA — Thu, 02 May 2013 07:51:20 GMT

←Older revision		Revision as of 07:51, 2 May 2013
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-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4hvv\| PDB=4hvv \| SCENE= }}
		+	===Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide APP12===

-	~~The entry 4hvv~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==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~~.	+	==About this Structure==
		+	[[4hvv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HVV OCA].

-	~~Description~~: ~~Crystal structure of the T98E c~~-~~Src~~-~~SH3 domain mutant in complex with the high affinity~~ peptide ~~APP12~~	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Gallus gallus]]
		+	[[Category: Non-specific protein-tyrosine kinase]]
		+	[[Category: Camara-Artigas, A.]]
		+	[[Category: Beta shandwich]]
		+	[[Category: Kinase]]
		+	[[Category: Proline rich motif]]
		+	[[Category: Sh3 like barrel]]
		+	[[Category: Signaling protein-peptide complex]]

OCA at 08:50, 2 January 2013

OCA — Wed, 02 Jan 2013 08:50:52 GMT

←Older revision		Revision as of 08:50, 2 January 2013
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	'''Unreleased structure'''		'''Unreleased structure'''

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

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

	Description: Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide APP12		Description: Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide APP12

OCA at 09:07, 21 November 2012

OCA — Wed, 21 Nov 2012 09:07:59 GMT

←Older revision		Revision as of 09:07, 21 November 2012
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	The entry 4hvv is ON HOLD		The entry 4hvv is ON HOLD

-	Authors: Camara-Artigas, A	+	Authors: Camara-Artigas, A.

	Description: Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide APP12		Description: Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide APP12

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

OCA — Wed, 14 Nov 2012 06:20:28 GMT

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

←Older revision

Revision as of 06:20, 14 November 2012

OCA: New page: '''Unreleased structure''' The entry 4hvv is ON HOLD Authors: Camara-Artigas, A Description: Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity pep...

OCA — Wed, 14 Nov 2012 06:20:27 GMT

New page: '''Unreleased structure''' The entry 4hvv is ON HOLD Authors: Camara-Artigas, A Description: Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity pep...

New page

'''Unreleased structure'''

The entry 4hvv is ON HOLD

Authors: Camara-Artigas, A

Description: Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide APP12