1gk5: Difference between revisions

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-[[Image:1gk5.gif|left|200px]]<br /><applet load="1gk5" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1gk5" />
-'''SOLUTION STRUCTURE THE MEGF/TGFALPHA44-50 CHIMERIC GROWTH FACTOR'''<br />
-==Overview==
+==Solution Structure the mEGF/TGFalpha44-50 chimeric growth factor==
-The solution structure of the growth factor chimera mEGF/TGFalpha44-50 has been determined using an extended version of the dyana procedure for calculating structures from NMR data. The backbone fold and preferred orientation of the domains of the chimera are similar to those found in previous studies of EGF structures, and several H-bonds used as input constraints in those studies were found independently in the chimera. This shows that the modified activity of the chimera does not result from a major structural change. However, the improved precision of the structure presented here allows the origin of some unusual chemical shifts found in all of these compounds to be explained, as well as the results obtained from some site-specific mutants. Further studies of the properties of this chimeric growth factor should help to elucidate the mechanism(s) of hetero- and homodimerization of the c-erbB receptors.
+<StructureSection load='1gk5' size='340' side='right'caption='[[1gk5]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1gk5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GK5 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=1gk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gk5 OCA], [https://pdbe.org/1gk5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gk5 RCSB], [https://www.ebi.ac.uk/pdbsum/1gk5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gk5 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/EGF_MOUSE EGF_MOUSE] EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6 (By similarity).[https://www.uniprot.org/uniprot/TGFA_HUMAN TGFA_HUMAN] TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor/EGFR and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar.
+== 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/gk/1gk5_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=1gk5 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-GK5 is a [http://en.wikipedia.org/wiki/Single_protein 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=1GK5 OCA].
+*[[Epidermal growth factor|Epidermal growth factor]]
+__TOC__
-==Reference==
+</StructureSection>
-Solution structure of the mEGF/TGFalpha44-50 chimeric growth factor., Chamberlin SG, Brennan L, Puddicombe SM, Davies DE, Turner DL, Eur J Biochem. 2001 Dec;268(23):6247-55. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11733021 11733021]
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Single protein]]
+[[Category: Brennan L]]
-[[Category: Brennan, L.]]
+[[Category: Chamberlin SG]]
-[[Category: Chamberlin, S G.]]
+[[Category: Davies DE]]
-[[Category: Davies, D E.]]
+[[Category: Puddicombe SM]]
-[[Category: Puddicombe, S M.]]
+[[Category: Turner DL]]
-[[Category: Turner, D L.]]
-[[Category: chimeric]]
-[[Category: egf growth factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:50:59 2008''