1ghu

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{{Seed}}
 
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[[Image:1ghu.png|left|200px]]
 
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==NMR solution structure of growth factor receptor-bound protein 2 (GRB2) SH2 domain, 24 structures==
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The line below this paragraph, containing "STRUCTURE_1ghu", creates the "Structure Box" on the page.
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<StructureSection load='1ghu' size='340' side='right'caption='[[1ghu]]' 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'>[[1ghu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GHU FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1ghu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghu OCA], [https://pdbe.org/1ghu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ghu RCSB], [https://www.ebi.ac.uk/pdbsum/1ghu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ghu ProSAT]</span></td></tr>
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{{STRUCTURE_1ghu| PDB=1ghu | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GRB2_HUMAN GRB2_HUMAN] Adapter protein that provides a critical link between cell surface growth factor receptors and the Ras signaling pathway.<ref>PMID:1322798</ref> <ref>PMID:8178156</ref> <ref>PMID:19815557</ref> Isoform 2 does not bind to phosphorylated epidermal growth factor receptor (EGFR) but inhibits EGF-induced transactivation of a RAS-responsive element. Isoform 2 acts as a dominant negative protein over GRB2 and by suppressing proliferative signals, may trigger active programmed cell death.<ref>PMID:1322798</ref> <ref>PMID:8178156</ref> <ref>PMID:19815557</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/gh/1ghu_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=1ghu 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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A family of NMR solution structures of the growth factor receptor-bound protein 2 (Grb2) SH2 domain has been determined by heteronuclear multidimensional NMR. Proton, nitrogen, and carbon chemical shift assignments have been made for the SH2 domain of Grb2. Assignments were made from a combination of homonuclear two-dimensional and 15N- and 13C-edited three-dimensional spectra at pH 6.2 and 298 K. Structure-induced proton and carbon secondary shifts were calculated and used to facilitate the spectral assignment process. NOE, scalar coupling, secondary chemical shift, and amide proton exchange data were used to characterize the secondary structural elements and hydrogen-bonding network in the Grb2 SH2 domain. The three-dimensional structure of the Grb2 SH2 domain was calculated using 1112 restraints obtained from NOE, coupling constant, and amide proton exchange data. The rmsd for the 24 calculated structures to the mean structure of the Grb2 SH2 domain was 0.75 A for backbone and 1.28 A for all heavy atoms. The three-dimensional fold of the Grb2 SH2 domain is similar to that observed for other SH2 domains and consists of two alpha-helical segments and eight beta-strands, six strands that make up two contiguous antiparallel beta-sheets, and two strands that form two short parallel beta-sheets. The structure of the phosphotyrosine binding pocket of Grb2 is similar to that observed for other SH2 domains. The hydrophobic binding pocket of Grb2 is similar to that observed for Src with the exception that tryptophan 121 of Grb2 occupies part of the pY+3 binding pocket. Structural implications for the Grb2 SH2 domain selectivity at the pY+2 and pY+3 sites are discussed.
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===NMR SOLUTION STRUCTURE OF GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2 (GRB2) SH2 DOMAIN, 24 STRUCTURES===
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Nuclear magnetic resonance solution structure of the growth factor receptor-bound protein 2 Src homology 2 domain.,Thornton KH, Mueller WT, McConnell P, Zhu G, Saltiel AR, Thanabal V Biochemistry. 1996 Sep 10;35(36):11852-64. PMID:8794768<ref>PMID:8794768</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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</div>
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<div class="pdbe-citations 1ghu" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_8794768}}, adds the Publication Abstract to the page
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*[[Growth factor receptor-bound proteins 3D structures|Growth factor receptor-bound proteins 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 8794768 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_8794768}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1GHU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHU OCA].
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==Reference==
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Nuclear magnetic resonance solution structure of the growth factor receptor-bound protein 2 Src homology 2 domain., Thornton KH, Mueller WT, McConnell P, Zhu G, Saltiel AR, Thanabal V, Biochemistry. 1996 Sep 10;35(36):11852-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8794768 8794768]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Mcconnell, P.]]
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[[Category: Mcconnell P]]
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[[Category: Mueller, W T.]]
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[[Category: Mueller WT]]
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[[Category: Saltiel, A R.]]
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[[Category: Saltiel AR]]
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[[Category: Thanabal, V.]]
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[[Category: Thanabal V]]
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[[Category: Thornton, K H.]]
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[[Category: Thornton KH]]
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[[Category: Zhu, G.]]
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[[Category: Zhu G]]
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[[Category: Grb2]]
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[[Category: Sh2]]
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[[Category: Src homology 2 domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:18:35 2008''
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Current revision

NMR solution structure of growth factor receptor-bound protein 2 (GRB2) SH2 domain, 24 structures

PDB ID 1ghu

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