1n52
From Proteopedia
(New page: 200px<br /> <applet load="1n52" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n52, resolution 2.11Å" /> '''Cap Binding Complex...) |
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| - | [[Image:1n52.gif|left|200px]]<br /> | + | [[Image:1n52.gif|left|200px]]<br /><applet load="1n52" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1n52, resolution 2.11Å" /> | caption="1n52, resolution 2.11Å" /> | ||
'''Cap Binding Complex'''<br /> | '''Cap Binding Complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 7-methyl guanosine cap structure of RNA is essential for key aspects | + | 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== | ==About this Structure== | ||
| - | 1N52 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG, GTG, PG4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1N52 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=GTG:'>GTG</scene>, <scene name='pdbligand=PG4:'>PG4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N52 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rnp domain]] | [[Category: rnp domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:19 2008'' |
Revision as of 12:02, 21 February 2008
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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 with , , and as ligands. 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 Thu Feb 21 14:02:19 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
