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1z9i

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[[Image:1z9i.gif|left|200px]]
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{{Seed}}
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[[Image:1z9i.png|left|200px]]
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{{STRUCTURE_1z9i| PDB=1z9i | SCENE= }}
{{STRUCTURE_1z9i| PDB=1z9i | SCENE= }}
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'''A Structural Model for the Membrane-Bound Form of the Juxtamembrane Domain of the Epidermal Growth Factor Receptor'''
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===A Structural Model for the Membrane-Bound Form of the Juxtamembrane Domain of the Epidermal Growth Factor Receptor===
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==Overview==
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The epidermal growth factor receptor (EGFR) is a member of the receptor tyrosine kinase family involved in the regulation of cellular proliferation and differentiation. Its juxtamembrane domain (JX), the region located between the transmembrane and kinase domains, plays important roles in receptor trafficking. Two sorting signals, a PXXP motif and a 658LL659 motif, are responsible for basolateral sorting in polarized epithelial cells, and a 679LL680 motif targets the ligand-activated receptor for lysosomal degradation. To understand the regulation of these signals, we characterized the structural properties of recombinant JX domain in aqueous solution and in dodecylphosphocholine (DPC) detergent. JX is inherently unstructured in aqueous solution, albeit a nascent helix encompasses the lysosomal sorting signal. In DPC micelles, structures derived from NMR data showed three amphipathic, helical segments. A large, internally inconsistent group of long range nuclear Overhauser effects suggest a close proximity of the helices, and the presence of significant conformational averaging. Models were determined for the average JX conformation using restraints representing the translational restriction due to micelle-surface adsorption, and the helix orientations were determined from residual dipolar couplings. Two equivalent average structural models were obtained that differ only in the relative orientation between first and second helices. In these models, the 658LL659 and 679LL680 motifs are located in the first and second helices and face the micelle surface, whereas the PXXP motif is located in a flexible helix-connecting region. The data suggest that the activity of these signals may be regulated by their membrane association and restricted accessibility in the intact receptor.
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The line below this paragraph, {{ABSTRACT_PUBMED_15840573}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15840573 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15840573}}
==About this Structure==
==About this Structure==
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1Z9I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z9I OCA].
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1Z9I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z9I OCA].
==Reference==
==Reference==
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[[Category: Sonnichsen, F D.]]
[[Category: Sonnichsen, F D.]]
[[Category: Juxtamembrane structure egfr micelle]]
[[Category: Juxtamembrane structure egfr micelle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:21:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:02:13 2008''

Revision as of 13:02, 27 July 2008

Image:1z9i.png

Template:STRUCTURE 1z9i

A Structural Model for the Membrane-Bound Form of the Juxtamembrane Domain of the Epidermal Growth Factor Receptor

Template:ABSTRACT PUBMED 15840573

About this Structure

1Z9I is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

A structural model for the membrane-bound form of the juxtamembrane domain of the epidermal growth factor receptor., Choowongkomon K, Carlin CR, Sonnichsen FD, J Biol Chem. 2005 Jun 24;280(25):24043-52. Epub 2005 Apr 19. PMID:15840573

Page seeded by OCA on Sun Jul 27 16:02:13 2008

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