1lf8: Difference between revisions

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[[Image:1lf8.~~gif~~|left|200px]]

[[Image:1lf8.png|left|200px]]

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~~'''~~Complex of GGA3-VHS Domain and CI-MPR C-terminal Phosphopeptide~~'''~~

===Complex of GGA3-VHS Domain and CI-MPR C-terminal Phosphopeptide===

~~==Overview==~~

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~~Phosphorylation of the cytosolic tails of transmembrane receptors can regulate their intracellular trafficking.~~ The ~~structural basis for such regulation~~, ~~however~~, ~~has not been explained in most cases. The cytosolic tail of~~ the ~~cation-independent mannose 6-phosphate receptor contains a serine residue within an acidic-cluster dileucine signal that is important for~~ the ~~function of the receptor in the biosynthetic sorting of lysosomal hydrolases~~. ~~We show here that phosphorylation of this Ser enhances interactions of the signal with its recognition module~~, the ~~VHS domain of the GGA proteins~~. Crystallographic analyses demonstrate that the phosphoserine residue interacts electrostatically with two basic residues on the VHS domain of GGA3, thus providing an additional point of attachment of the acidic-~~cluster dileucine signal to its recognition module.~~

The line below this paragraph, {{ABSTRACT_PUBMED_12032548}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12032548 is the PubMed ID number.

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==About this Structure==

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[[Category: Protein-phosphopeptide complex]]

[[Category: Vhs domain]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 23:52:04 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 18:36:11 2008''

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-[[Image:1lf8.gif|left|200px]]
+{{Seed}}
+[[Image:1lf8.png|left|200px]]
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 {{STRUCTURE_1lf8|  PDB=1lf8  |  SCENE=  }}
-'''Complex of GGA3-VHS Domain and CI-MPR C-terminal Phosphopeptide'''
+===Complex of GGA3-VHS Domain and CI-MPR C-terminal Phosphopeptide===
-==Overview==
+<!--
-Phosphorylation of the cytosolic tails of transmembrane receptors can regulate their intracellular trafficking. The structural basis for such regulation, however, has not been explained in most cases. The cytosolic tail of the cation-independent mannose 6-phosphate receptor contains a serine residue within an acidic-cluster dileucine signal that is important for the function of the receptor in the biosynthetic sorting of lysosomal hydrolases. We show here that phosphorylation of this Ser enhances interactions of the signal with its recognition module, the VHS domain of the GGA proteins. Crystallographic analyses demonstrate that the phosphoserine residue interacts electrostatically with two basic residues on the VHS domain of GGA3, thus providing an additional point of attachment of the acidic-cluster dileucine signal to its recognition module.
+The line below this paragraph, {{ABSTRACT_PUBMED_12032548}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12032548 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12032548}}
 ==About this Structure==
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 [[Category: Protein-phosphopeptide complex]]
 [[Category: Vhs domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:52:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 18:36:11 2008''