Sandbox Reserved 708: Difference between revisions

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This structure also possesses <scene name='Sandbox_Reserved_708/Mg_ions/3'>two divalent cations Mg2+</scene> as well as <scene name='Sandbox_Reserved_708/Adp/3'>two molecules of ADP</scene>(Adenosine DiPhosphate). Arg-141 is one of the key residues for <scene name='Sandbox_Reserved_708/Adp_recognition_by_arg141/1'>specific ATP/ADP recognition</scene> by GSK3,<ref name="SINR"/>.  
This structure also possesses <scene name='Sandbox_Reserved_708/Mg_ions/3'>two divalent cations Mg2+</scene> as well as <scene name='Sandbox_Reserved_708/Adp/3'>two molecules of ADP</scene>(Adenosine DiPhosphate). Arg-141 is one of the key residues for <scene name='Sandbox_Reserved_708/Adp_recognition_by_arg141/1'>specific ATP/ADP recognition</scene> by GSK3,<ref name="SINR"/>.  


These are the <scene name='Sandbox_Reserved_708/Catalytic_site/7'>amino acids</scene> engaged in the catalytic site of the protein, they are polar and localised in 3' end: Asp-181, Lys-183, Gln-185, Asn-186 and Ser-219.  
The <scene name='Sandbox_Reserved_708/Catalytic_site/7'>amino acids</scene> engaged in the catalytic site of the protein are Asp-181, Lys-183, Gln-185, Asn-186 and Ser-219. They are polar and localised in 3' end.  


This enzyme is activated by phosphorylation on <scene name='Sandbox_Reserved_708/Tyr-216_phosphorylation/3'>Tyr-216</scene> and inactivated by phosphorylation on Ser-9 (not shown here because this structure starts at residue 35). But the phosphorylation on Tyr-216 is not mandatory for the activity,<ref>"Crystal Structure of Glycogen Synthase Kinase 3β: Structural Basis for Phosphate-Primed Substrate Specificity and Autoinhibition" Rana Dajani, Elizabeth Fraser, S. Mark Roe, Neville Young, Valerie Good, Trevor C. Dale and Laurence H. Pearl1; Cell, Vol. 105, 721–732, June 15, 2001, Copyright 2001 by Cell Press</ref>.
This enzyme is activated by phosphorylation on <scene name='Sandbox_Reserved_708/Tyr-216_phosphorylation/3'>Tyr-216</scene> and inactivated by phosphorylation on Ser-9 (not shown here because the solved structure starts at residue 35). But the phosphorylation on Tyr-216 is not mandatory for the activity,<ref>"Crystal Structure of Glycogen Synthase Kinase 3β: Structural Basis for Phosphate-Primed Substrate Specificity and Autoinhibition" Rana Dajani, Elizabeth Fraser, S. Mark Roe, Neville Young, Valerie Good, Trevor C. Dale and Laurence H. Pearl1; Cell, Vol. 105, 721–732, June 15, 2001, Copyright 2001 by Cell Press</ref>.




This structure possesse 2 domains according to the CATH structural classification:
This structure has 2 domains according to the CATH structural classification:
*<scene name='Sandbox_Reserved_708/Cath_domain_1j1ca01/1'>CATH Domain 1j1cA01</scene> [http://www.cathdb.info/version/latest/domain/1j1cA01]
*<scene name='Sandbox_Reserved_708/Cath_domain_1j1ca01/1'>CATH Domain 1j1cA01</scene> [http://www.cathdb.info/version/latest/domain/1j1cA01]
*<scene name='Sandbox_Reserved_708/Cath_domain_1j1ca02/1'>CATH Domain 1j1cA02</scene> [http://www.cathdb.info/version/latest/domain/1j1cA02]
*<scene name='Sandbox_Reserved_708/Cath_domain_1j1ca02/1'>CATH Domain 1j1cA02</scene> [http://www.cathdb.info/version/latest/domain/1j1cA02]

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OCA, Noémie Kunkler, Fabienne Dricot
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