1obx: Difference between revisions

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[[Image:1obx.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ2 OF SYNTENIN WITH AN INTERLEUKIN 5 RECEPTOR ALPHA PEPTIDE.~~'''~~

===CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ2 OF SYNTENIN WITH AN INTERLEUKIN 5 RECEPTOR ALPHA PEPTIDE.===

~~==Overview==~~

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~~Crystal structures of the PDZ2 domain of the scaffolding protein syntenin~~, ~~both unbound and in complexes with peptides derived from C termini of IL5 receptor (alpha chain) and syndecan~~, ~~reveal~~ the ~~molecular roots of syntenin's degenerate specificity. Three distinct binding sites~~ (~~S(0), S(-1), and S(-2)), with affinities for hydrophobic side chains, function in a combinatorial way~~: ~~S(-1~~) ~~and S(-2) act together to bind syndecan~~, ~~while S(0) and S(-1) are involved in~~ the ~~binding of IL5Ralpha~~. ~~Neither mode of interaction is consistent with the prior classification scheme, which defined the IL5Ralpha interaction as class I (-S/T~~-X-phi) and the syndecan interaction as class II (-phi-X-phi). These results, in conjunction with other emerging structural data on PDZ domains, call for a revision of their classification and of the existing model of their mechanism.

The line below this paragraph, {{ABSTRACT_PUBMED_12842047}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12842047 is the PubMed ID number.

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==About this Structure==

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[[Category: Pdz domain]]

[[Category: Signal transduction,nuclear protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 03~~:38:48 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:15:16 2008''

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-[[Image:1obx.gif|left|200px]]
+{{Seed}}
+[[Image:1obx.png|left|200px]]
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 {{STRUCTURE_1obx|  PDB=1obx  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ2 OF SYNTENIN WITH AN INTERLEUKIN 5 RECEPTOR ALPHA PEPTIDE.'''
+===CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ2 OF SYNTENIN WITH AN INTERLEUKIN 5 RECEPTOR ALPHA PEPTIDE.===
-==Overview==
+<!--
-Crystal structures of the PDZ2 domain of the scaffolding protein syntenin, both unbound and in complexes with peptides derived from C termini of IL5 receptor (alpha chain) and syndecan, reveal the molecular roots of syntenin's degenerate specificity. Three distinct binding sites (S(0), S(-1), and S(-2)), with affinities for hydrophobic side chains, function in a combinatorial way: S(-1) and S(-2) act together to bind syndecan, while S(0) and S(-1) are involved in the binding of IL5Ralpha. Neither mode of interaction is consistent with the prior classification scheme, which defined the IL5Ralpha interaction as class I (-S/T-X-phi) and the syndecan interaction as class II (-phi-X-phi). These results, in conjunction with other emerging structural data on PDZ domains, call for a revision of their classification and of the existing model of their mechanism.
+The line below this paragraph, {{ABSTRACT_PUBMED_12842047}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12842047 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12842047}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Pdz domain]]
 [[Category: Signal transduction,nuclear protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:38:48 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:15:16 2008''