3ov1

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{{STRUCTURE_3ov1| PDB=3ov1 | SCENE= }}
 
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===Crystal Structure of the Grb2 SH2 Domain in Complex with a pYXN-Derived Tripeptide===
 
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{{ABSTRACT_PUBMED_22007755}}
 
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==About this Structure==
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==Crystal Structure of the Grb2 SH2 Domain in Complex with a pYXN-Derived Tripeptide==
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[[3ov1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OV1 OCA].
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<StructureSection load='3ov1' size='340' side='right'caption='[[3ov1]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3ov1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OV1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OV1 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]] 1.6&#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=1AC:1-AMINOCYCLOPROPANECARBOXYLIC+ACID'>1AC</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></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=3ov1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ov1 OCA], [https://pdbe.org/3ov1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ov1 RCSB], [https://www.ebi.ac.uk/pdbsum/3ov1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ov1 ProSAT]</span></td></tr>
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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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Thermodynamic parameters were determined for complex formation between the Grb2 SH2 domain and Ac-pTyr-Xaa-Asn derived tripeptides in which the Xaa residue is an alpha,alpha-cycloaliphatic amino acid that varies in ring size from three- to seven-membered. Although the six- and seven-membered ring analogs are approximately equipotent, binding affinities of those having three- to six-membered rings increase incrementally with ring size because increasingly more favorable binding enthalpies dominate increasingly less favorable binding entropies, a finding consistent with an enthalpy-driven hydrophobic effect. Crystallographic analysis reveals that the only significant differences in structures of the complexes are in the number of van der Waals contacts between the domain and the methylene groups in the Xaa residues. There is a positive correlation between buried nonpolar surface area and binding free energy and enthalpy, but not with DeltaC(p). Displacing a water molecule from a protein-ligand interface is not necessarily reflected in a favorable change in binding entropy. These findings highlight some of the fallibilities associated with commonly held views of relationships of structure and energetics in protein-ligand interactions and have significant implications for ligand design.
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==See Also==
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Protein-Ligand Interactions: Thermodynamic Effects Associated with Increasing Nonpolar Surface Area.,Myslinski JM, Delorbe JE, Clements JH, Martin SF J Am Chem Soc. 2011 Oct 27. PMID:22007755<ref>PMID:22007755</ref>
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*[[Growth factor receptor-bound protein|Growth factor receptor-bound protein]]
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:022007755</ref><references group="xtra"/>
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</div>
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<div class="pdbe-citations 3ov1" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Growth factor receptor-bound proteins 3D structures|Growth factor receptor-bound proteins 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Clements, J H.]]
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[[Category: Large Structures]]
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[[Category: Martin, S F.]]
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[[Category: Clements JH]]
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[[Category: Grb2 sh2 domain]]
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[[Category: Martin SF]]
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[[Category: Phosphotyrosine binding]]
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[[Category: Signaling protein]]
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[[Category: Signaling protein-antagonist complex]]
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Current revision

Crystal Structure of the Grb2 SH2 Domain in Complex with a pYXN-Derived Tripeptide

PDB ID 3ov1

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