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1lf8
From Proteopedia
Revision as of 14:28, 28 September 2014 by OCA (Talk | contribs)
1lf8 is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism.,Kato Y, Misra S, Puertollano R, Hurley JH, Bonifacino JS Nat Struct Biol. 2002 Jul;9(7):532-6. PMID:12032548[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Kato Y, Misra S, Puertollano R, Hurley JH, Bonifacino JS. Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism. Nat Struct Biol. 2002 Jul;9(7):532-6. PMID:12032548 doi:10.1038/nsb807
