1n52
From Proteopedia
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|PDB= 1n52 |SIZE=350|CAPTION= <scene name='initialview01'>1n52</scene>, resolution 2.11Å | |PDB= 1n52 |SIZE=350|CAPTION= <scene name='initialview01'>1n52</scene>, resolution 2.11Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=GTG:7-METHYL-GUANOSINE-5 | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=GTG:7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-GUANOSINE'>GTG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= CBP80 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), CBP20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= CBP80 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), CBP20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
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[[Category: rnp domain]] | [[Category: rnp domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:51:24 2008'' |
Revision as of 10:51, 23 March 2008
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| , resolution 2.11Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Gene: | CBP80 (Homo sapiens), CBP20 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Cap Binding Complex
Overview
The 7-methyl guanosine cap structure of RNA is essential for key aspects of RNA processing, including pre-mRNA splicing, 3' end formation, U snRNA transport, nonsense-mediated decay and translation. Two cap-binding proteins mediate these effects: cytosolic eIF-4E and nuclear cap-binding protein complex (CBC). The latter consists of a CBP20 subunit, which binds the cap, and a CBP80 subunit, which ensures high-affinity cap binding. Here we report the 2.1 A resolution structure of human CBC with the cap analog m7GpppG, as well as the structure of unliganded CBC. Comparisons between these structures indicate that the cap induces substantial conformational changes within the N-terminal loop of CBP20, enabling Tyr 20 to join Tyr 43 in pi-pi stacking interactions with the methylated guanosine base. CBP80 stabilizes the movement of the N-terminal loop of CBP20 and locks the CBC into a high affinity cap-binding state. The structure for the CBC bound to m7GpppG highlights interesting similarities and differences between CBC and eIF-4E, and provides insights into the regulatory mechanisms used by growth factors and other extracellular stimuli to influence the cap-binding state of the CBC.
About this Structure
1N52 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis of m7GpppG binding to the nuclear cap-binding protein complex., Calero G, Wilson KF, Ly T, Rios-Steiner JL, Clardy JC, Cerione RA, Nat Struct Biol. 2002 Dec;9(12):912-7. PMID:12434151
Page seeded by OCA on Sun Mar 23 12:51:24 2008
Categories: Homo sapiens | Protein complex | Calero, G. | Cerione, R. | Clardy, J. | Ly, T. | Rios-Steiner, J. | Wilson, K. | GOL | GTG | MG | PG4 | Cap binding protein | Cbp20 | Cbp80 | M7gpppg | Rnp domain
