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Comparative modeling of the N-terminal domain of the 67kDa laminin-binding protein: implications for putative

Dmitri A Kazmin1, Yurii Chinenov, Eric Larson

  • 1Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA.

Biochemical and Biophysical Research Communications
|December 14, 2002
PubMed

Insights

Laminin-binding protein/p40 (LBP/p40) has a dual role in cell adhesion and ribosomal biogenesis. Structural modeling suggests these functions may be mutually exclusive due to domain overlap.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Structural Biology

Background:

  • Laminin-binding protein/p40 (LBP/p40) precursor exhibits dual functions in cell adhesion and ribosomal biogenesis.
  • LBP/p40 possesses a two-domain structure: an N-terminal domain similar to prokaryotic ribosomal protein S2 and a unique Metazoan C-terminal domain for extraribosomal functions.

Purpose of the Study:

  • To investigate the putative ribosomal functions of LBP/p40.
  • To elucidate the structural basis for LBP/p40's bifunctionality through comparative modeling.

Main Methods:

  • Comparative modeling of the LBP/p40 N-terminal domain using crystal structures of Thermus thermophilus S2p.
  • Analysis of structural features, including fold, rRNA interaction domains, surface charge distribution, and potential transmembrane domains.

Main Results:

  • The LBP/p40 N-terminal domain model adopts an alpha-beta sandwich fold, similar to S2.
  • Significant loss of rRNA interaction domains and altered surface charge distribution compared to S2 were observed.
  • The protein's fold stability contradicts a proposed transmembrane domain.
  • Partial overlap between S2 and laminin-binding domains was identified.

Conclusions:

  • The structural analysis suggests that ribosomal and cell adhesion functions of LBP/p40 are likely mutually exclusive.
  • The study provides insights into the structural constraints and potential biological implications of LBP/p40's bifunctionality.

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