2v5e

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{{Seed}}
 
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[[Image:2v5e.png|left|200px]]
 
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==The structure of the GDNF:Coreceptor complex: Insights into RET signalling and heparin binding.==
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The line below this paragraph, containing "STRUCTURE_2v5e", creates the "Structure Box" on the page.
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<StructureSection load='2v5e' size='340' side='right'caption='[[2v5e]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2v5e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V5E FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GU4:2,3,4,6-TETRA-O-SULFONATO-ALPHA-D-GLUCOPYRANOSE'>GU4</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900013:sucrose+octasulfate'>PRD_900013</scene>, <scene name='pdbligand=YYJ:1,3,4,6-tetra-O-sulfo-beta-D-fructofuranose'>YYJ</scene></td></tr>
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{{STRUCTURE_2v5e| PDB=2v5e | SCENE= }}
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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=2v5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v5e OCA], [https://pdbe.org/2v5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v5e RCSB], [https://www.ebi.ac.uk/pdbsum/2v5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v5e ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GFRA1_RAT GFRA1_RAT] Receptor for GDNF. Mediates the GDNF-induced autophosphorylation and activation of the RET receptor.
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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/v5/2v5e_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=2v5e 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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Glial cell line-derived neurotrophic factor (GDNF), a neuronal survival factor, binds its co-receptor GDNF family receptor alpha1 (GFR alpha 1) in a 2:2 ratio and signals through the receptor tyrosine kinase RET. We have solved the GDNF(2).GFR alpha 1(2) complex structure at 2.35 A resolution in the presence of a heparin mimic, sucrose octasulfate. The structure of our GDNF(2).GFR alpha 1(2) complex and the previously published artemin(2).GFR alpha 3(2) complex are unlike in three ways. First, we have experimentally identified residues that differ in the ligand-GFR alpha interface between the two structures, in particular ones that buttress the key conserved Arg(GFR alpha)-Glu(ligand)-Arg(GFR alpha) interaction. Second, the flexible GDNF ligand "finger" loops fit differently into the GFR alphas, which are rigid. Third, and we believe most importantly, the quaternary structure of the two tetramers is dissimilar, because the angle between the two GDNF monomers is different. This suggests that the RET-RET interaction differs in different ligand(2)-co-receptor(2)-RET(2) heterohexamer complexes. Consistent with this, we showed that GDNF(2).GFR alpha1(2) and artemin(2).GFR alpha 3(2) signal differently in a mitogen-activated protein kinase assay. Furthermore, we have shown by mutagenesis and enzyme-linked immunosorbent assays of RET phosphorylation that RET probably interacts with GFR alpha 1 residues Arg-190, Lys-194, Arg-197, Gln-198, Lys-202, Arg-257, Arg-259, Glu-323, and Asp-324 upon both domains 2 and 3. Interestingly, in our structure, sucrose octasulfate also binds to the Arg(190)-Lys(202) region in GFR alpha 1 domain 2. This may explain how GDNF.GFR alpha 1 can mediate cell adhesion and how heparin might inhibit GDNF signaling through RET.
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===THE STRUCTURE OF THE GDNF\:CORECEPTOR COMPLEX\: INSIGHTS INTO RET SIGNALLING AND HEPARIN BINDING.===
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The structure of the glial cell line-derived neurotrophic factor-coreceptor complex: insights into RET signaling and heparin binding.,Parkash V, Leppanen VM, Virtanen H, Jurvansuu JM, Bespalov MM, Sidorova YA, Runeberg-Roos P, Saarma M, Goldman A J Biol Chem. 2008 Dec 12;283(50):35164-72. Epub 2008 Oct 8. PMID:18845535<ref>PMID:18845535</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_18845535}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2v5e" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18845535 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18845535}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2V5E is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5E OCA].
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==Reference==
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The structure of the GDNF:Coreceptor complex: Insights into RET signalling and heparin binding., Parkash V, Leppanen VM, Virtanen H, Jurvansuu JM, Bespalov MM, Sidorova YA, Runeberg-Roos P, Saarma M, Goldman A, J Biol Chem. 2008 Oct 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18845535 18845535]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Bespalov, M M.]]
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[[Category: Bespalov MM]]
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[[Category: Goldman, A.]]
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[[Category: Goldman A]]
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[[Category: Jurvansuu, J M.]]
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[[Category: Jurvansuu J-M]]
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[[Category: Leppanen, V M.]]
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[[Category: Leppanen V-M]]
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[[Category: Parkash, V.]]
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[[Category: Parkash V]]
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[[Category: Runeberg-Roos, P.]]
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[[Category: Runeberg-Roos P]]
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[[Category: Saarma, M.]]
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[[Category: Saarma M]]
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[[Category: Sidorova, Y A.]]
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[[Category: Sidorova YA]]
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[[Category: Virtanen, H.]]
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[[Category: Virtanen H]]
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[[Category: Alternative splicing]]
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[[Category: Cell membrane]]
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[[Category: Cleavage on pair of basic residue]]
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[[Category: Gdnf]]
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[[Category: Gfralpha1]]
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[[Category: Glycoprotein]]
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[[Category: Gpi-anchor]]
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[[Category: Growth factor]]
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[[Category: Ligand-coreceptor]]
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[[Category: Lipoprotein]]
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[[Category: Membrane]]
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[[Category: Polymorphism]]
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[[Category: Receptor]]
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[[Category: Receptor/glycoprotein complex]]
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[[Category: Ret]]
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[[Category: Secreted]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 17 13:00:40 2008''
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Current revision

The structure of the GDNF:Coreceptor complex: Insights into RET signalling and heparin binding.

PDB ID 2v5e

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