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3bs5

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[[Image:3bs5.png|left|200px]]
 
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{{STRUCTURE_3bs5| PDB=3bs5 | SCENE= }}
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==Crystal Structure of hCNK2-SAM/dHYP-SAM Complex==
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<StructureSection load='3bs5' size='340' side='right'caption='[[3bs5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3bs5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BS5 FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bs7|3bs7]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ave ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), CNKSR2, CNK2, KIAA0902, KSR2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bs5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bs5 OCA], [https://pdbe.org/3bs5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bs5 RCSB], [https://www.ebi.ac.uk/pdbsum/3bs5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bs5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/AVE_DROME AVE_DROME]] Required for normal photoreceptor differentiation between Ras and Raf for EGFR signaling in the eye and for mitogen-activated protein kinase phosphorylation. Probably acts together with Cnk to promote Raf activation, perhaps by recruiting an activating kinase. [[https://www.uniprot.org/uniprot/CNKR2_HUMAN CNKR2_HUMAN]] May function as an adapter protein or regulator of Ras signaling pathways.<ref>PMID:14597674</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bs/3bs5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bs5 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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RAF kinase functions in the mitogen-activated protein kinase (MAPK) pathway to transmit growth signals to the downstream kinases MEK and ERK. Activation of RAF catalytic activity is facilitated by a regulatory complex comprising the proteins CNK (Connector enhancer of KSR), HYP (Hyphen), and KSR (Kinase Suppressor of Ras). The sterile alpha-motif (SAM) domain found in both CNK and HYP plays an essential role in complex formation. Here, we have determined the x-ray crystal structure of the SAM domain of CNK in complex with the SAM domain of HYP. The structure reveals a single-junction SAM domain dimer of 1:1 stoichiometry in which the binding mode is a variation of polymeric SAM domain interactions. Through in vitro and in vivo mutational analyses, we show that the specific mode of dimerization revealed by the crystal structure is essential for RAF signaling and facilitates the recruitment of KSR to form the CNK/HYP/KSR regulatory complex. We present two docking-site models to account for how SAM domain dimerization might influence the formation of a higher-order CNK/HYP/KSR complex.
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===Crystal Structure of hCNK2-SAM/dHYP-SAM Complex===
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CNK and HYP form a discrete dimer by their SAM domains to mediate RAF kinase signaling.,Rajakulendran T, Sahmi M, Kurinov I, Tyers M, Therrien M, Sicheri F Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):2836-41. Epub 2008 Feb 19. PMID:18287031<ref>PMID:18287031</ref>
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{{ABSTRACT_PUBMED_18287031}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 3bs5" style="background-color:#fffaf0;"></div>
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[[3bs5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BS5 OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:018287031</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Drosophila melanogaster]]
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[[Category: Drome]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Ceccarelli, D F.]]
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[[Category: Large Structures]]
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[[Category: Kurinov, I.]]
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[[Category: Ceccarelli, D F]]
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[[Category: Rajakulendran, T.]]
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[[Category: Kurinov, I]]
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[[Category: Sicheri, F.]]
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[[Category: Rajakulendran, T]]
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[[Category: Sicheri, F]]
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[[Category: Alternative splicing]]
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[[Category: Coiled coil]]
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[[Category: Cytoplasm]]
[[Category: Membrane]]
[[Category: Membrane]]
[[Category: Phosphoprotein]]
[[Category: Phosphoprotein]]
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[[Category: Polymorphism]]
[[Category: Sam domain]]
[[Category: Sam domain]]
[[Category: Sam domain complex]]
[[Category: Sam domain complex]]

Current revision

Crystal Structure of hCNK2-SAM/dHYP-SAM Complex

PDB ID 3bs5

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