1gk5: Difference between revisions
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==Solution Structure the mEGF/TGFalpha44-50 chimeric growth factor== | |||
<StructureSection load='1gk5' size='340' side='right' caption='[[1gk5]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='1gk5' size='340' side='right' caption='[[1gk5]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gk5]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GK5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1gk5]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GK5 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gk5 OCA], [http://pdbe.org/1gk5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gk5 RCSB], [http://www.ebi.ac.uk/pdbsum/1gk5 PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gk5 OCA], [http://pdbe.org/1gk5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gk5 RCSB], [http://www.ebi.ac.uk/pdbsum/1gk5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gk5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 07:34, 21 September 2017
Solution Structure the mEGF/TGFalpha44-50 chimeric growth factorSolution Structure the mEGF/TGFalpha44-50 chimeric growth factor
Structural highlights
Function[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). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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:11733021[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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