View source for 2kv4


==EGF==
<StructureSection load='2kv4' size='340' side='right'caption='[[2kv4]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2kv4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KV4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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=2kv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kv4 OCA], [https://pdbe.org/2kv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kv4 RCSB], [https://www.ebi.ac.uk/pdbsum/2kv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kv4 ProSAT]</span></td></tr>
</table>
== 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 ==
[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> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human epidermal growth factor (hEGF) induces the proliferation, differentiation and survival of various cell types including tumor-derived cells. Generally, hEGF performs its biological function by binding to a specific receptor (hEGFR) on the cell surface, thereby inducing signal transduction. Suramin, a polysulfonated naphthylurea that acts as a growth factor blocker, exhibits antiproliferative activity against non-small cell lung cancer (NSCLC) cells that overexpress EGFR on the cell surface. We determined the solution structure of hEGF under physiological conditions and investigated the interaction of suramin with hEGF using isothermal titration calorimetry and NMR spectroscopy techniques. The solution structure of hEGF presented in this paper is different from the bound form of hEGF present in the crystal structure of the 2:2 EGF-EGFR complex because its C-tail contains a hydrophobic core. This conformational difference supports the hypothesis that hEGF undergoes a conformational change when it binds to hEGFR and subsequently induces signal transduction. Based on the docking structure of the hEGF-suramin complex, we demonstrated how suramin blocks hEGF by binding to its receptor binding site (the C-terminal region around Arg45) and inhibits the crucial conformational change.

The NMR solution structure of human epidermal growth factor (hEGF) at physiological pH and its interactions with suramin.,Huang HW, Mohan SK, Yu C Biochem Biophys Res Commun. 2010 Nov 26;402(4):705-10. Epub 2010 Oct 26. PMID:21029725<ref>PMID:21029725</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2kv4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Epidermal growth factor|Epidermal growth factor]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Huang HW]]
[[Category: Mohan SK]]
[[Category: Yu C]]