1q2h

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(New page: 200px<br /> <applet load="1q2h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q2h, resolution 1.70&Aring;" /> '''Phenylalanine Zippe...)
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[[Image:1q2h.gif|left|200px]]<br />
 
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<applet load="1q2h" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1q2h, resolution 1.70&Aring;" />
 
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'''Phenylalanine Zipper Mediates APS Dimerization'''<br />
 
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==Overview==
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==Phenylalanine Zipper Mediates APS Dimerization==
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The APS, SH2-B and LNK proteins are adapters that activate and modulate, receptor tyrosine kinase and JAK/STAT signaling. We now show that a, conserved N-terminal domain mediates APS homodimerization. We determined, the crystal structure of the dimerization domain at a resolution of 1.7 A, using bromide ion MAD phasing. Each molecule contributes two helices to a, compact four-helix bundle having a bisecting-U topology. Its most, conspicuous feature is a stack of interdigitated phenylalanine side chains, at the domain core. These residues create a new motif we refer to as a, 'phenylalanine zipper,' which is critical to dimerization. A newly, developed bridging yeast tri-hybrid assay showed that APS dimerizes JAK2, insulin receptor and IGF1 receptor kinases using its SH2 and dimerization, domains. Dimerization via the phenylalanine zipper domain provides a, mechanism for activating and modulating tyrosine kinase activity even in, the absence of extracellular ligands.
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<StructureSection load='1q2h' size='340' side='right'caption='[[1q2h]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1q2h]] is a 3 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=1Q2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q2H 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]] 1.7&#8491;</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=1q2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q2h OCA], [https://pdbe.org/1q2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q2h RCSB], [https://www.ebi.ac.uk/pdbsum/1q2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q2h ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SH2B2_HUMAN SH2B2_HUMAN] Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways. May be involved in coupling from immunoreceptor to Ras signaling. Acts as a negative regulator of cytokine signaling in collaboration with CBL. Binds to EPOR and suppresses EPO-induced STAT5 activation, possibly through a masking effect on STAT5 docking sites in EPOR. Suppresses PDGF-induced mitogenesis. May induce cytoskeletal reorganization via interaction with VAV3.<ref>PMID:10374881</ref> <ref>PMID:9989826</ref> <ref>PMID:12400014</ref> <ref>PMID:15378031</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/q2/1q2h_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=1q2h 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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The APS, SH2-B and LNK proteins are adapters that activate and modulate receptor tyrosine kinase and JAK/STAT signaling. We now show that a conserved N-terminal domain mediates APS homodimerization. We determined the crystal structure of the dimerization domain at a resolution of 1.7 A using bromide ion MAD phasing. Each molecule contributes two helices to a compact four-helix bundle having a bisecting-U topology. Its most conspicuous feature is a stack of interdigitated phenylalanine side chains at the domain core. These residues create a new motif we refer to as a 'phenylalanine zipper,' which is critical to dimerization. A newly developed bridging yeast tri-hybrid assay showed that APS dimerizes JAK2, insulin receptor and IGF1 receptor kinases using its SH2 and dimerization domains. Dimerization via the phenylalanine zipper domain provides a mechanism for activating and modulating tyrosine kinase activity even in the absence of extracellular ligands.
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==About this Structure==
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A phenylalanine zipper mediates APS dimerization.,Dhe-Paganon S, Werner ED, Nishi M, Hansen L, Chi YI, Shoelson SE Nat Struct Mol Biol. 2004 Oct;11(10):968-74. Epub 2004 Sep 19. PMID:15378031<ref>PMID:15378031</ref>
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1Q2H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q2H OCA].
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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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A phenylalanine zipper mediates APS dimerization., Dhe-Paganon S, Werner ED, Nishi M, Hansen L, Chi YI, Shoelson SE, Nat Struct Mol Biol. 2004 Oct;11(10):968-74. Epub 2004 Sep 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15378031 15378031]
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</div>
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<div class="pdbe-citations 1q2h" style="background-color:#fffaf0;"></div>
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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: Single protein]]
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[[Category: Large Structures]]
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[[Category: Chi, Y.I.]]
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[[Category: Chi Y-I]]
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[[Category: Dhe-Paganon, S.]]
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[[Category: Dhe-Paganon S]]
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[[Category: Nishi, M.]]
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[[Category: Nishi M]]
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[[Category: Shoelson, S.E.]]
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[[Category: Shoelson SE]]
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[[Category: Werner, E.D.]]
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[[Category: Werner ED]]
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[[Category: signal transduction]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:49:46 2007''
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Current revision

Phenylalanine Zipper Mediates APS Dimerization

PDB ID 1q2h

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