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[[ | ==Crystal structure of ERK2/DCC peptide complex== | ||
<StructureSection load='3o71' size='340' side='right' caption='[[3o71]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3o71]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O71 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O71 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mapk1, Erk2, Mapk, Prkm1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mitogen-activated_protein_kinase Mitogen-activated protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.24 2.7.11.24] </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=3o71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o71 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o71 RCSB], [http://www.ebi.ac.uk/pdbsum/3o71 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Netrin receptor DCC plays critical roles in many cellular processes, including axonal outgrowth and migration, angiogenesis, and apoptosis, but the molecular basis of DCC-mediated signaling is largely unclear. ERK2, a member of the MAPK family, is one of the few proteins known to be involved in DCC-mediated signaling. Here, we report that ERK2 directly interacts with DCC, and the ERK2-binding region was mapped to the conserved intracellular P1 domain of the receptor. The structure of ERK2 in complex with the P1 domain of DCC reveals that DCC contains a MAPK docking motif. The docking of the P1 domain onto ERK2 physically positions several phosphorylation sites of DCC in the vicinity of the kinase active site. We further show that the docking interaction between the P1 domain and ERK2 is essential for the ERK2-mediated phosphorylation of DCC. We conclude that DCC signaling is directly coupled with MAPK signaling cascades. | |||
Phosphorylation of DCC by ERK2 is facilitated by direct docking of the receptor P1 domain to the kinase.,Ma W, Shang Y, Wei Z, Wen W, Wang W, Zhang M Structure. 2010 Nov 10;18(11):1502-11. PMID:21070949<ref>PMID:21070949</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Mitogen-activated protein kinase|Mitogen-activated protein kinase]] | *[[Mitogen-activated protein kinase|Mitogen-activated protein kinase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Mitogen-activated protein kinase]] | [[Category: Mitogen-activated protein kinase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Ma, W F | [[Category: Ma, W F]] | ||
[[Category: Shang, Y | [[Category: Shang, Y]] | ||
[[Category: Wang, W N | [[Category: Wang, W N]] | ||
[[Category: Wei, Z Y | [[Category: Wei, Z Y]] | ||
[[Category: Wen, W Y | [[Category: Wen, W Y]] | ||
[[Category: Zhang, M J | [[Category: Zhang, M J]] | ||
[[Category: Dcc]] | [[Category: Dcc]] | ||
[[Category: Kinase]] | [[Category: Kinase]] | ||
[[Category: Protein-peptide complex]] | [[Category: Protein-peptide complex]] | ||
[[Category: Transferase-protein binding complex]] | [[Category: Transferase-protein binding complex]] | ||
Revision as of 15:30, 9 December 2014
Crystal structure of ERK2/DCC peptide complexCrystal structure of ERK2/DCC peptide complex
Structural highlights
Publication Abstract from PubMedNetrin receptor DCC plays critical roles in many cellular processes, including axonal outgrowth and migration, angiogenesis, and apoptosis, but the molecular basis of DCC-mediated signaling is largely unclear. ERK2, a member of the MAPK family, is one of the few proteins known to be involved in DCC-mediated signaling. Here, we report that ERK2 directly interacts with DCC, and the ERK2-binding region was mapped to the conserved intracellular P1 domain of the receptor. The structure of ERK2 in complex with the P1 domain of DCC reveals that DCC contains a MAPK docking motif. The docking of the P1 domain onto ERK2 physically positions several phosphorylation sites of DCC in the vicinity of the kinase active site. We further show that the docking interaction between the P1 domain and ERK2 is essential for the ERK2-mediated phosphorylation of DCC. We conclude that DCC signaling is directly coupled with MAPK signaling cascades. Phosphorylation of DCC by ERK2 is facilitated by direct docking of the receptor P1 domain to the kinase.,Ma W, Shang Y, Wei Z, Wen W, Wang W, Zhang M Structure. 2010 Nov 10;18(11):1502-11. PMID:21070949[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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