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The structure of BRMS1 nuclear export signal and SNX6 interacting region reveals a hexamer formed by antiparallel

Mercedes Spínola-Amilibia1, José Rivera, Miguel Ortiz-Lombardía

  • 1Instituto de Biomedicina de Valencia (IBV-CSIC), C/ Jaime Roig 11, 46010 Valencia, Spain.

Journal of Molecular Biology
|July 23, 2011
PubMed

Insights

Breast cancer metastasis suppressor 1 (BRMS1) protein

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cancer Research

Background:

  • Metastasis suppressor proteins, like BRMS1, are crucial as they inhibit cancer spread without impacting primary tumor growth.
  • The N-terminal region of BRMS1 is implicated in molecular interactions, cellular localization, and transcriptional repression.
  • Understanding BRMS1's structure is key to elucidating its metastasis-suppressing mechanisms.

Purpose of the Study:

  • To determine the three-dimensional structure of the N-terminal region of breast cancer metastasis suppressor 1 (BRMS1).
  • To investigate the oligomeric state and structural features of BRMS1(51-98).
  • To explore how the structural characteristics of the BRMS1 N-terminus contribute to its biological functions.

Main Methods:

  • X-ray crystallography was employed to determine the high-resolution structure of the BRMS1 N-terminal region.
  • Hydrodynamic experiments were conducted to assess the quaternary structure of BRMS1(51-98) in solution.

Main Results:

  • The crystal structure revealed that residues 51-98 of BRMS1 form an antiparallel coiled-coil motif.
  • BRMS1(51-98) was found to homo-oligomerize into a hexameric conformation, specifically a trimer of coiled-coil dimers.
  • Hydrodynamic experiments corroborated the prevalence of this hexameric quaternary structure in solution.

Conclusions:

  • The N-terminal coiled-coil region of BRMS1 is structurally characterized as an antiparallel motif capable of forming hexamers.
  • These findings suggest that BRMS1's ability to promote molecular clustering via its N-terminal coiled-coil may influence its biological functions, including metastasis suppression.
  • The study provides structural insights into BRMS1, aiding in the understanding of its role in cancer biology.

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