1jl9
From Proteopedia
(Difference between revisions)
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<StructureSection load='1jl9' size='340' side='right'caption='[[1jl9]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1jl9' size='340' side='right'caption='[[1jl9]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1jl9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1jl9]] 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=1JL9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JL9 FirstGlance]. <br> |
| - | </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=1jl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jl9 OCA], [https://pdbe.org/1jl9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jl9 RCSB], [https://www.ebi.ac.uk/pdbsum/1jl9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jl9 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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=1jl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jl9 OCA], [https://pdbe.org/1jl9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jl9 RCSB], [https://www.ebi.ac.uk/pdbsum/1jl9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jl9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | + | [https://www.uniprot.org/uniprot/EGF_HUMAN EGF_HUMAN] Defects in EGF are the cause of hypomagnesemia type 4 (HOMG4) [MIM:[https://omim.org/entry/611718 611718]; also known as renal hypomagnesemia normocalciuric. HOMG4 is a disorder characterized by massive renal hypomagnesemia and normal levels of serum calcium and calcium excretion. Clinical features include seizures, mild-to mederate psychomotor retardation, and brisk tendon reflexes.<ref>PMID:17671655</ref> | |
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/EGF_HUMAN EGF_HUMAN] 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.<ref>PMID:17671655</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1jl9 ConSurf]. | </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=1jl9 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Epidermal growth factor (EGF) is a typical growth-stimulating peptide and functions by binding to specific cell-surface receptors and inducing dimerization of the receptors. Little is known about the molecular mechanism of EGF-induced dimerization of EGF receptors. The crystal structure of human EGF has been determined at pH 8.1. There are two human EGF molecules A and B in the asymmetric unit of the crystals, which form a potential dimer. Importantly, a number of residues known to be indispensable for EGF binding to its receptor are involved in the interface between the two EGF molecules, suggesting a crucial role of EGF dimerization in the EGF-induced dimerization of receptors. In addition, the crystal structure of EGF shares the main features of the NMR structure of mouse EGF determined at pH 2.0, but structural comparisons between different models have revealed new detailed features and properties of the EGF structure. | ||
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| - | Crystal structure of human epidermal growth factor and its dimerization.,Lu HS, Chai JJ, Li M, Huang BR, He CH, Bi RC J Biol Chem. 2001 Sep 14;276(37):34913-7. Epub 2001 Jul 3. PMID:11438527<ref>PMID:11438527</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1jl9" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Bi | + | [[Category: Bi RC]] |
| - | [[Category: Chai | + | [[Category: Chai JJ]] |
| - | [[Category: He | + | [[Category: He CH]] |
| - | [[Category: Huang | + | [[Category: Huang BR]] |
| - | [[Category: Li | + | [[Category: Li M]] |
| - | [[Category: Lu | + | [[Category: Lu HS]] |
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Revision as of 07:52, 3 April 2024
Crystal Structure of Human Epidermal Growth Factor
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Categories: Homo sapiens | Large Structures | Bi RC | Chai JJ | He CH | Huang BR | Li M | Lu HS
