3c0h: Difference between revisions

Revision as of 18:09, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3c0h.png

Template:STRUCTURE 3c0h

CASK CaM-Kinase Domain- AMPPNP complex, P1 formCASK CaM-Kinase Domain- AMPPNP complex, P1 form

Template:ABSTRACT PUBMED 18423203

About this StructureAbout this Structure

3C0H is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

CASK Functions as a Mg2+-independent neurexin kinase., Mukherjee K, Sharma M, Urlaub H, Bourenkov GP, Jahn R, Sudhof TC, Wahl MC, Cell. 2008 Apr 18;133(2):328-39. PMID:18423203

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''CASK CaM-Kinase Domain- AMPPNP complex, P1 form'''
+===CASK CaM-Kinase Domain- AMPPNP complex, P1 form===
-==Overview==
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-CASK is a unique MAGUK protein that contains an N-terminal CaM-kinase domain besides the typical MAGUK domains. The CASK CaM-kinase domain is presumed to be a catalytically inactive pseudokinase because it lacks the canonical DFG motif required for Mg2+ binding that is thought to be indispensable for kinase activity. Here we show, however, that CASK functions as an active protein kinase even without Mg2+ binding. High-resolution crystal structures reveal that the CASK CaM-kinase domain adopts a constitutively active conformation that binds ATP and catalyzes phosphotransfer without Mg2+. The CASK CaM-kinase domain phosphorylates itself and at least one physiological interactor, the synaptic protein neurexin-1, to which CASK is recruited via its PDZ domain. Thus, our data indicate that CASK combines the scaffolding activity of MAGUKs with an unusual kinase activity that phosphorylates substrates recuited by the scaffolding activity. Moreover, our study suggests that other pseudokinases (10% of the kinome) could also be catalytically active.
+The line below this paragraph, {{ABSTRACT_PUBMED_18423203}}, adds the Publication Abstract to the page
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 [[Category: Synaptic plasticity]]
 [[Category: Transferase]]
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