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Related Experiment Videos

Structural basis of m7GpppG binding to the nuclear cap-binding protein complex.

Guillermo Calero1, Kristin F Wilson, Thi Ly

  • 1Department of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, New York 14853, USA.

Nature Structural Biology
|November 16, 2002
PubMed
Summary

The nuclear cap-binding complex (CBC) structure reveals how it binds RNA's 7-methyl guanosine cap. This binding involves conformational changes in CBP20, stabilized by CBP80, crucial for RNA processing.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • The 7-methyl guanosine cap is vital for RNA processing, including splicing, translation, and decay.
  • Cytosolic eIF-4E and nuclear cap-binding protein complex (CBC) mediate these cap-dependent functions.
  • CBC comprises CBP20 (cap-binding subunit) and CBP80 (high-affinity binding subunit).

Purpose of the Study:

  • To determine the high-resolution structure of human CBC bound to the cap analog m7GpppG.
  • To elucidate the structural basis of cap recognition and binding affinity by CBC.
  • To compare the structure of CBC with and without the cap analog.

Main Methods:

  • X-ray crystallography was used to determine the structure of human CBC.
  • Structures were solved at 2.1 Å resolution for both cap-bound and unliganded CBC.

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  • Comparative structural analysis was performed between the two states.

    • Main Results:

    • The cap analog m7GpppG induces significant conformational changes in the CBP20 N-terminal loop.
    • Specific tyrosine residues (Tyr 20 and Tyr 43) in CBP20 engage in pi-pi stacking with the methylated guanosine base.
    • CBP80 stabilizes these conformational changes, locking CBC into a high-affinity cap-binding state.
    • Structural comparisons revealed similarities and differences between CBC and eIF-4E.

    Conclusions:

    • The structure provides atomic-level insights into how CBC recognizes and binds the 7-methyl guanosine cap.
    • Understanding CBC's cap-binding mechanism sheds light on regulatory pathways influenced by extracellular signals.
    • These findings are crucial for comprehending fundamental RNA processing events and their regulation.