User:Iris To/Retinoblastoma Protein Regulation: Difference between revisions
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==Structure and Function== | ==Structure and Function== | ||
PP1[http://www.signaling-gateway.org/update/images/su-0406-3-i1.jpg]has an N-terminal, α/β domain, and a C-terminal β domain. The β domains come together as a <scene name='User:Iris_To/Retinoblastoma_Protein_Regulation/Rb_cterm_binding/7'>β-sandwich</scene>. The catalytic site is inside a a large Y-shaped cleft made by the three domains. Grooves are made by the domains: a hydrophobic, acidic, and C-terminal groove<ref>Terrak, Mohammed, Kerff, Frederic, Langsetmo, Knut, Tao, Terence, & Dominguez, Roberto Structural basis of protein phosphatase 1 regulation. Nature, 429, 780–784 (17 June 2004); 10.1038/nature02582</ref>. Rb866-889 is required for binding with PP1c; Rb870-882 is required for PP1c association with all of the significant interacting residues. Rb 870-882 also contains the Cyclin A docking site and KLRF sequence(like RVxF motif) where kinase and phosphatase compete. | PP1[http://www.signaling-gateway.org/update/images/su-0406-3-i1.jpg]has an N-terminal, α/β domain, and a C-terminal β domain. The β domains come together as a <scene name='User:Iris_To/Retinoblastoma_Protein_Regulation/Rb_cterm_binding/7'>β-sandwich</scene>. The catalytic site is inside a a large Y-shaped cleft made by the three domains. Grooves are made by the domains: a hydrophobic, acidic, and C-terminal groove<ref>Terrak, Mohammed, Kerff, Frederic, Langsetmo, Knut, Tao, Terence, & Dominguez, Roberto Structural basis of protein phosphatase 1 regulation. Nature, 429, 780–784 (17 June 2004); 10.1038/nature02582</ref>. Rb866-889 is required for binding with PP1c; Rb870-882 is required for PP1c association with all of the significant interacting residues. Rb 870-882 also contains the Cyclin A docking site and KLRF sequence(like RVxF motif) where kinase and phosphatase compete. | ||
<scene name='User:Iris_To/Retinoblastoma_Protein_Regulation/Rb_cterm_binding/2'>Rb binds PP1c with an extended conformation at hydrophobic interface</scene> of the β-sandwich subdomain, which is <scene name='User:Iris_To/Retinoblastoma_Protein_Regulation/Rb_cterm_binding/5'>away from phosphatase active site</scene>. <scene name='User:Iris_To/Retinoblastoma_Protein_Regulation/Rb_cterm_binding/3'>Arg876,Phe877,Asp877 form</scene> a <scene name='User:Iris_To/Retinoblastoma_Protein_Regulation/Rb_cterm_binding/6'>short β-strand</scene> that becomes part of sheet 1 of the PP1c β-sandwich subdomain, with hydrogen bonding interactions with the parallel adjacent strand. | <scene name='User:Iris_To/Retinoblastoma_Protein_Regulation/Rb_cterm_binding/2'>Rb binds PP1c with an extended conformation at hydrophobic interface</scene> of the β-sandwich subdomain, which is <scene name='User:Iris_To/Retinoblastoma_Protein_Regulation/Rb_cterm_binding/5'>away from phosphatase active site</scene><ref name=Hirschi>PMID: 20694007</ref>. <scene name='User:Iris_To/Retinoblastoma_Protein_Regulation/Rb_cterm_binding/3'>Arg876,Phe877,Asp877 form</scene> a <scene name='User:Iris_To/Retinoblastoma_Protein_Regulation/Rb_cterm_binding/6'>short β-strand</scene> that becomes part of sheet 1 of the PP1c β-sandwich subdomain, with hydrogen bonding interactions with the parallel adjacent strand. | ||
<scene name='User:Iris_To/Retinoblastoma_Protein_Regulation/Rb_cterm_binding/4'>Leu875 and Phe877</scene> are hydrophobic, and they insert into the pocket of the hydrophobic groove of PP1c. These two also bind to the hydrophobic pockets in CycA in RbC-Cdk2-CycA. Their insertion is important in the stabilization of the interaction between the phosphatase or kinase and substrate. | <scene name='User:Iris_To/Retinoblastoma_Protein_Regulation/Rb_cterm_binding/4'>Leu875 and Phe877</scene> are hydrophobic, and they insert into the pocket of the hydrophobic groove of PP1c. These two also bind to the hydrophobic pockets in CycA in RbC-Cdk2-CycA. Their insertion is important in the stabilization of the interaction between the phosphatase or kinase and substrate<ref name=Hirschi>PMID: 20694007</ref>. | ||
</StructureSection> | </StructureSection> | ||
