This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Journal:JBIC:2
From Proteopedia
(Difference between revisions)
| (43 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | < | + | <StructureSection load='3rec' size='350' side='right' caption='' scene='Journal:JBIC:2/Opening/1'> |
===Structure of Anticancer Ruthenium Half-Sandwich Complex Bound to Glycogen Synthase Kinase 3ß=== | ===Structure of Anticancer Ruthenium Half-Sandwich Complex Bound to Glycogen Synthase Kinase 3ß=== | ||
| - | <big>G. Atilla-Gocumen, L. Di Costanzo, E. Meggers</big> | + | <big>G. Atilla-Gocumen, L. Di Costanzo, E. Meggers</big> <ref>DOI 10.1007/s00775-010-0699-x</ref> |
<hr/> | <hr/> | ||
| + | <b>Molecular Tour</b><br> | ||
| + | A crystal structure of an <scene name='Journal:JBIC:2/Half_sandwich_complex_no_bonds/1'>organometallic half-sandwich ruthenium complex</scene> bound to the protein kinase glycogen synthase kinase 3ß (GSK-3ß) has been determined (PDB entry [[3m1s]]) and reveals that the inhibitor binds to the <scene name='Journal:JBIC:2/Atp_binding_site2/2'>ATP binding site</scene> via an induced fit mechanism utlizing several <scene name='Journal:JBIC:2/Half_sandwich_complex/3'>hydrogen bonds</scene> and <scene name='Journal:JBIC:2/Half_sandwich_hydrophobic_stic/1'>hydrophobic interactions</scene>. Importantly, the metal is not involved in any direct interaction with the protein kinase but fulfills a purely structural role. The unique, bulky molecular structure of the half-sandwich complex with the CO-ligand oriented perpendicular to the pyridocarbazole heterocycle allows the complex to stretch the whole distance <scene name='Journal:JBIC:2/Half_sandwich_hydrophobic/5'>sandwiched between the faces of the N- and C-terminal lobes</scene> and to interact tightly with <scene name='Journal:JBIC:2/Glycine_rich_loop2/4'>the flexible glycine-rich loop</scene>. Although this complex is a conventional ATP-competitive binder, the unique shape of the complex allows novel interactions with the glycine-rich loop which are crucial for binding potency and selectivity. It can be hypothesized that coordination spheres which present other ligands towards the glycine-rich loop might display completely different protein kinase selectivities. | ||
| - | + | '''PDB reference:''' Structure of Ruthenium Half-Sandwich Complex Bound to Glycogen Synthase Kinase 3, [[3m1s]]. | |
| + | <b>References</b><br> | ||
<references/> | <references/> | ||
| + | </StructureSection> | ||
__NOEDITSECTION__ | __NOEDITSECTION__ | ||
Current revision
| |||||||||||
Proteopedia Page Contributors and Editors (what is this?)
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
