1J1B
Binary complex structure of human tau protein kinase I with AMPPNP
Summary for 1J1B
Entry DOI | 10.2210/pdb1j1b/pdb |
Related | 1J1C |
Descriptor | Glycogen synthase kinase-3 beta, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (3 entities in total) |
Functional Keywords | complex, tau, kinase, amppnp, transferase |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm: P49841 |
Total number of polymer chains | 2 |
Total formula weight | 94614.82 |
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 Cited by 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: 14993667DOI: 10.1107/S090744490302938X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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