1dnr: Difference between revisions
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{{Theoretical_model}} | {{Theoretical_model}} | ||
< | ==THEORETICAL MODEL OF THE THIRD AND FOURTH DOMAINS OF THE HUMAN EPIDERMAL GROWTH FACTOR RECEPTOR ECTODOMAIN== | ||
<StructureSection load='1dnr' size='340' side='right'caption='[[1dnr]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DNR 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=1dnr FirstGlance], [https://www.ebi.ac.uk/pdbsum/1dnr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dnr ProSAT]</span></td></tr> | |||
- | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Epidermal Growth Factor (EGF) receptor is a tyrosine kinase that mediates the biological effects of ligands such as EGF and transforming growth factor alpha. An understanding of the molecular basis of its action has been hindered by a lack of structural and mutational data on the receptor. We have constructed comparative models of the four extracellular domains of the EGF receptor that are based on the structure of the first three domains of the insulin-like growth factor-1 (IGF-1) receptor. The first and third domains of the EGF receptor, L1 and L2, are right-handed beta helices. The second and fourth domains of the EGF receptor, S1 and S2, consist of the modules held together by disulfide bonds, which, except for the first module of the S1 domain, form rod-like structures. The arrangement of the L1 and S1 domains of the model are similar to that of the first two domains of the IGF-1 receptor, whereas that of the L2 and S2 domains appear to be significantly different. Using the EGF receptor model and limited information from the literature, we have proposed a number of regions that may be involved in the functioning of the receptor. In particular, the faces containing the large beta sheets in the L1 and L2 domains have been suggested to be involved with ligand binding of EGF to its receptor. | |||
Characterization of a comparative model of the extracellular domain of the epidermal growth factor receptor.,Jorissen RN, Epa VC, Treutlein HR, Garrett TP, Ward CW, Burgess AW Protein Sci. 2000 Feb;9(2):310-24. PMID:10716183<ref>PMID:10716183</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1dnr" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Theoretical Model]] | ||
[[Category: Large Structures]] | |||
== | |||
< | |||
[[Category: Burgess, A W]] | [[Category: Burgess, A W]] | ||
[[Category: Epa, V C]] | [[Category: Epa, V C]] | ||
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[[Category: Treutlein, H R]] | [[Category: Treutlein, H R]] | ||
[[Category: Ward, C W]] | [[Category: Ward, C W]] | ||
Latest revision as of 12:29, 21 July 2021
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THEORETICAL MODEL OF THE THIRD AND FOURTH DOMAINS OF THE HUMAN EPIDERMAL GROWTH FACTOR RECEPTOR ECTODOMAINTHEORETICAL MODEL OF THE THIRD AND FOURTH DOMAINS OF THE HUMAN EPIDERMAL GROWTH FACTOR RECEPTOR ECTODOMAIN
Structural highlights
Publication Abstract from PubMedThe Epidermal Growth Factor (EGF) receptor is a tyrosine kinase that mediates the biological effects of ligands such as EGF and transforming growth factor alpha. An understanding of the molecular basis of its action has been hindered by a lack of structural and mutational data on the receptor. We have constructed comparative models of the four extracellular domains of the EGF receptor that are based on the structure of the first three domains of the insulin-like growth factor-1 (IGF-1) receptor. The first and third domains of the EGF receptor, L1 and L2, are right-handed beta helices. The second and fourth domains of the EGF receptor, S1 and S2, consist of the modules held together by disulfide bonds, which, except for the first module of the S1 domain, form rod-like structures. The arrangement of the L1 and S1 domains of the model are similar to that of the first two domains of the IGF-1 receptor, whereas that of the L2 and S2 domains appear to be significantly different. Using the EGF receptor model and limited information from the literature, we have proposed a number of regions that may be involved in the functioning of the receptor. In particular, the faces containing the large beta sheets in the L1 and L2 domains have been suggested to be involved with ligand binding of EGF to its receptor. Characterization of a comparative model of the extracellular domain of the epidermal growth factor receptor.,Jorissen RN, Epa VC, Treutlein HR, Garrett TP, Ward CW, Burgess AW Protein Sci. 2000 Feb;9(2):310-24. PMID:10716183[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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