1nql: Difference between revisions

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~~'''~~Structure of the extracellular domain of human epidermal growth factor (EGF) receptor in an inactive (low pH) complex with EGF.~~'''~~

===Structure of the extracellular domain of human epidermal growth factor (EGF) receptor in an inactive (low pH) complex with EGF.===

~~==Overview==~~

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~~Epidermal growth factor (EGF) receptor is~~ the ~~prototype of~~ the ~~ErbB (HER) family receptor tyrosine kinases~~ (RTKs), which regulate cell growth and differentiation and are implicated in many human cancers. EGF activates its receptor by inducing dimerization of the 621 amino acid EGF receptor extracellular region. ~~We describe the 2~~.~~8 A resolution crystal structure of this entire extracellular region (sEGFR~~) ~~in an unactivated state. The structure reveals an autoinhibited configuration~~, where ~~the dimerization interface recently identified in activated sEGFR structures~~ is ~~completely occluded by intramolecular interactions. To activate~~ the receptor, EGF binding must promote a large domain rearrangement that exposes this dimerization interface. This contrasts starkly with other RTK activation mechanisms and suggests new approaches for designing ErbB receptor antagonists.

The line below this paragraph, {{ABSTRACT_PUBMED_12620237}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12620237 is the PubMed ID number.

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==Disease==

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[[Category: Growth factor]]

[[Category: Tyrosine kinase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 02~~:51:50 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:43:06 2008''

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-[[Image:1nql.jpg|left|200px]]
+{{Seed}}
+[[Image:1nql.png|left|200px]]
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 {{STRUCTURE_1nql|  PDB=1nql  |  SCENE=  }}
-'''Structure of the extracellular domain of human epidermal growth factor (EGF) receptor in an inactive (low pH) complex with EGF.'''
+===Structure of the extracellular domain of human epidermal growth factor (EGF) receptor in an inactive (low pH) complex with EGF.===
-==Overview==
+<!--
-Epidermal growth factor (EGF) receptor is the prototype of the ErbB (HER) family receptor tyrosine kinases (RTKs), which regulate cell growth and differentiation and are implicated in many human cancers. EGF activates its receptor by inducing dimerization of the 621 amino acid EGF receptor extracellular region. We describe the 2.8 A resolution crystal structure of this entire extracellular region (sEGFR) in an unactivated state. The structure reveals an autoinhibited configuration, where the dimerization interface recently identified in activated sEGFR structures is completely occluded by intramolecular interactions. To activate the receptor, EGF binding must promote a large domain rearrangement that exposes this dimerization interface. This contrasts starkly with other RTK activation mechanisms and suggests new approaches for designing ErbB receptor antagonists.
+The line below this paragraph, {{ABSTRACT_PUBMED_12620237}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12620237 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12620237}}
 ==Disease==
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 [[Category: Growth factor]]
 [[Category: Tyrosine kinase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:51:50 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:43:06 2008''