1fhs: Difference between revisions
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New page: left|200px<br /> <applet load="1fhs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fhs" /> '''THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF... |
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== | ==THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY DOMAIN-2 OF THE GROWTH FACTOR RECEPTOR BOUND PROTEIN-2, NMR, 18 STRUCTURES== | ||
<StructureSection load='1fhs' size='340' side='right'caption='[[1fhs]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1fhs]] 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=1FHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FHS FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1fhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fhs OCA], [https://pdbe.org/1fhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fhs RCSB], [https://www.ebi.ac.uk/pdbsum/1fhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fhs ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/1fhs_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1fhs ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A set of high-resolution three-dimensional solution structures of the Src homology region-2 (SH2) domain of the growth factor receptor-bound protein-2 was determined using heteronuclear NMR spectroscopy. The NMR data used in this study were collected on a stable monomeric protein solution that was free of protein aggregates and proteolysis. The solution structure was determined based upon a total of 1439 constraints, which included 1326 nuclear Overhauser effect distance constraints, 70 hydrogen bond constraints, and 43 dihedral angle constraints. Distance geometry-simulated annealing calculations followed by energy minimization yielded a family of 18 structures that converged to a root-mean-square deviation of 1.09 A for all backbone atoms and 0.40 A for the backbone atoms of the central beta-sheet. The core structure of the SH2 domain contains an antiparallel beta-sheet flanked by two parallel alpha-helices displaying an overall architecture that is similar to other known SH2 domain structures. This family of NMR structures is compared to the X-ray structure and to another family of NMR solution structures determined under different solution conditions. | |||
The three-dimensional solution structure of the SRC homology domain-2 of the growth factor receptor-bound protein-2.,Senior MM, Frederick AF, Black S, Murgolo NJ, Perkins LM, Wilson O, Snow ME, Wang YS J Biomol NMR. 1998 Feb;11(2):153-64. doi: 10.1023/A:1008250309874. PMID:20700826<ref>PMID:20700826</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1fhs" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Growth factor receptor-bound proteins 3D structures|Growth factor receptor-bound proteins 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Black | [[Category: Black S]] | ||
[[Category: Frederick | [[Category: Frederick AF]] | ||
[[Category: Perkins | [[Category: Perkins LM]] | ||
[[Category: Senior | [[Category: Senior MM]] | ||
[[Category: Snow | [[Category: Snow ME]] | ||
[[Category: Wang | [[Category: Wang Y-S]] | ||
[[Category: Wilson | [[Category: Wilson O]] | ||
