1J1C

Binary complex structure of human tau protein kinase I with ADP

Summary for 1J1C

• Entry DOI: 10.2210/pdb1j1c/pdb
• Related: 1J1B
• Descriptor: Glycogen synthase kinase-3 beta, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: complex, tau, kinase, adp, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P49841
• Total number of polymer chains: 2
• Total formula weight: 94505.44

Authors

Aoki, M.,Yokota, T.,Sugiura, I.,Sasaki, C.,Hasegawa, T.,Okumura, C.,Kohno, T.,Sugio, S.,Matsuzaki, T. (deposition date: 2002-12-03, release date: 2003-12-03, Last modification date: 2023-12-27)

Primary citation

Aoki, M.,Yokota, T.,Sugiura, I.,Sasaki, C.,Hasegawa, T.,Okumura, C.,Ishiguro, K.,Kohno, T.,Sugio, S.,Matsuzaki, T.
Structural insight into nucleotide recognition in tau-protein kinase I/glycogen synthase kinase 3 beta.
Acta Crystallogr.,Sect.D, 60:439-446, 2004

PubMed Abstract: Human tau-protein kinase I (TPK I; also known as glycogen synthase kinase 3 beta; GSK3 beta) is a serine/threonine protein kinase that participates in Alzheimer's disease. Here, binary complex structures of full-length TPK I/GSK3 beta with the ATP analogues ADP and AMPPNP solved by the X-ray diffraction method at 2.1 and 1.8 A resolution, respectively, are reported. TPK I/GSK3 beta is composed of three domains: an N-terminal domain consisting of a closed beta-barrel structure, a C-terminal domain containing a 'kinase fold' structure and a small extra-domain subsequent to the C-terminal domain. The catalytic site is between the two major domains and has an ATP-analogue molecule in its ATP-binding site. The adenine ring is buried in the hydrophobic pocket and interacts specifically with the main-chain atoms of the hinge loop. The overall structure and substrate-binding residues are similar to those observed in other Ser/Thr protein kinases, while Arg141 (which is not conserved among other Ser/Thr protein kinases) is one of the key residues for specific ATP/ADP recognition by TPK I/GSK3 beta. No residues are phosphorylated, while the orientation of the activation loop in TPK I/GSK3 beta is similar to that in phosphorylated CDK2 and ERK2, suggesting that TPK I/GSK3 beta falls into a conformation that enables it to be constitutively active.

PubMed: 14993667
DOI: 10.1107/S090744490302938X

Experimental method

X-RAY DIFFRACTION (2.1 Å)