1j1c
From Proteopedia
(New page: 200px<br /> <applet load="1j1c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j1c, resolution 2.1Å" /> '''Binary complex struc...) |
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| - | [[Image:1j1c.gif|left|200px]]<br /> | + | [[Image:1j1c.gif|left|200px]]<br /><applet load="1j1c" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1j1c" size=" | + | |
caption="1j1c, resolution 2.1Å" /> | caption="1j1c, resolution 2.1Å" /> | ||
'''Binary complex structure of human tau protein kinase I with ADP'''<br /> | '''Binary complex structure of human tau protein kinase I with ADP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Human tau-protein kinase I (TPK I; also known as glycogen synthase kinase | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1J1C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http:// | + | 1J1C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J1C OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tau]] | [[Category: tau]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:17:53 2008'' |
Revision as of 11:17, 21 February 2008
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Binary complex structure of human tau protein kinase I with ADP
Overview
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.
About this Structure
1J1C is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
Structural insight into nucleotide recognition in tau-protein kinase I/glycogen synthase kinase 3 beta., Aoki M, Yokota T, Sugiura I, Sasaki C, Hasegawa T, Okumura C, Ishiguro K, Kohno T, Sugio S, Matsuzaki T, Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):439-46. Epub 2004, Feb 25. PMID:14993667
Page seeded by OCA on Thu Feb 21 13:17:53 2008
Categories: Homo sapiens | Non-specific serine/threonine protein kinase | Single protein | Aoki, M. | Hasegawa, T. | Kohno, T. | Matsuzaki, T. | Okumura, C. | Sasaki, C. | Sugio, S. | Sugiura, I. | Yokota, T. | ADP | MG | Adp | Complex | Kinase | Tau
