4btm: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4btm|  PDB=4btm  |  SCENE=  }}
===TTBK1 in complex with inhibitor===
{{ABSTRACT_PUBMED_24039150}}


The entry 4btm is ON HOLD
==Function==
[[http://www.uniprot.org/uniprot/TTBK1_HUMAN TTBK1_HUMAN]] Serine/threonine kinase which is able to phosphorylate TAU on serine, threonine and tyrosine residues. Induces aggregation of TAU.<ref>PMID:16923168</ref> 


Authors: Xue, Y., Wan, P., Hillertz, P., Schweikart, F., Zhao, Y., Wissler, L., Dekker, N.
==About this Structure==
[[4btm]] is a 2 chain structure with 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=4BTM OCA].  


Description: TTBK1 in complex with inhibitor
==Reference==
<ref group="xtra">PMID:024039150</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Dekker, N.]]
[[Category: Hillertz, P.]]
[[Category: Schweikart, F.]]
[[Category: Wan, P.]]
[[Category: Wissler, L.]]
[[Category: Xue, Y.]]
[[Category: Zhao, Y.]]
[[Category: Ligand complex]]
[[Category: Structure-kinetics relationship]]
[[Category: Transferase]]

Revision as of 08:11, 29 September 2013

Template:STRUCTURE 4btm

TTBK1 in complex with inhibitor

Template:ABSTRACT PUBMED 24039150

Function

[TTBK1_HUMAN] Serine/threonine kinase which is able to phosphorylate TAU on serine, threonine and tyrosine residues. Induces aggregation of TAU.[1]

About this Structure

4btm is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  1. Xue Y, Wan PT, Hillertz P, Schweikart F, Zhao Y, Wissler L, Dekker N. X-ray Structural Analysis of Tau-Tubulin Kinase 1 and Its Interactions with Small Molecular Inhibitors. ChemMedChem. 2013 Sep 13. doi: 10.1002/cmdc.201300274. PMID:24039150 doi:10.1002/cmdc.201300274
  1. Sato S, Cerny RL, Buescher JL, Ikezu T. Tau-tubulin kinase 1 (TTBK1), a neuron-specific tau kinase candidate, is involved in tau phosphorylation and aggregation. J Neurochem. 2006 Sep;98(5):1573-84. PMID:16923168 doi:JNC4059

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