1i0c: Difference between revisions

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-{{Seed}}
-[[Image:1i0c.png|left|200px]]
-<!--
+==EPS8 SH3 CLOSED MONOMER==
-The line below this paragraph, containing "STRUCTURE_1i0c", creates the "Structure Box" on the page.
+<StructureSection load='1i0c' size='340' side='right'caption='[[1i0c]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1i0c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I0C FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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&#8491;</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=1i0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i0c OCA], [https://pdbe.org/1i0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i0c RCSB], [https://www.ebi.ac.uk/pdbsum/1i0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i0c ProSAT]</span></td></tr>
-{{STRUCTURE_1i0c|  PDB=1i0c  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/EPS8_MOUSE EPS8_MOUSE] Upon binding to EGF receptor/EGFR enhances EGF-dependent mitogenic signals. Can bind multiple cellular targets.<ref>PMID:8404850</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/i0/1i0c_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=1i0c ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The SH3 domain of Eps8 was previously found to form an intertwined, domain-swapped dimer. We report here a monomeric structure of the EPS8 SH3 domain obtained from crystals grown at low pH, as well as an improved domain-swapped dimer structure at 1.8 A resolution. In the domain-swapped dimer the asymmetric unit contains two "hybrid-monomers." In the low pH form there are two independently folded SH3 molecules per asymmetric unit. The formation of intermolecular salt bridges is thought to be the reason for the formation of the dimer. On the basis of the monomer SH3 structure, it is argued that Eps8 SH3 should, in principle, bind to peptides containing a PxxP motif. Recently it was reported that Eps8 SH3 binds to a peptide with a PxxDY motif. Because the "SH3 fold" is conserved, alternate binding sites may be possible for the PxxDY motif to bind. The strand exchange or domain swap occurs at the n-src loops because the n-src loops are flexible. The thermal b-factors also indicate the flexible nature of n-src loops and a possible handle for domain swap initiation. Despite the loop swapping, the typical SH3 fold in both forms is conserved structurally. The interface of the acidic form of SH3 is stabilized by a tetragonal network of water molecules above hydrophobic residues. The intertwined dimer interface is stabilized by hydrophobic and aromatic stacking interactions in the core and by hydrophilic interactions on the surface.
-===EPS8 SH3 CLOSED MONOMER===
+Effect of pH and salt bridges on structural assembly: molecular structures of the monomer and intertwined dimer of the Eps8 SH3 domain.,Kishan KV, Newcomer ME, Rhodes TH, Guilliot SD Protein Sci. 2001 May;10(5):1046-55. PMID:11316885<ref>PMID:11316885</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_11316885}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1i0c" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11316885 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11316885}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-I0C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I0C OCA].
-==Reference==
-Effect of pH and salt bridges on structural assembly: molecular structures of the monomer and intertwined dimer of the Eps8 SH3 domain., Kishan KV, Newcomer ME, Rhodes TH, Guilliot SD, Protein Sci. 2001 May;10(5):1046-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11316885 11316885]
 [[Category: Mus musculus]]
-[[Category: Single protein]]
+[[Category: Kishan KVR]]
-[[Category: Kishan, K V.R.]]
+[[Category: Newcomer ME]]
-[[Category: Newcomer, M E.]]
-[[Category: Hormone/growth factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 10:13:10 2008''