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August 14, 2026Journal of Molecular BiologyOpen Access

Coiled-Coil Domain Kinking Controls Laminin-332 Cleavage by Elastase

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Authors

LALucky AkterRARomain AmyotRGRobert Großmann

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Overview

In vitro structural study reveals that coiled-coil kinking directs elastase cleavage in laminin-332, highlighting a conformational mechanism governing basement membrane protein processing.

Key Points

  • Investigate the structural dynamics of the laminin-332 coiled-coil domain and determine how conformational flexibility regulates its proteolytic cleavage by elastase.
  • Combined high-speed atomic force microscopy (HS-AFM) time-lapse imaging with AlphaFold structural predictions and normal-mode flexible fitting to model hinge dynamics at atomic resolution.
  • Visualized real-time digestion of individual laminin-332 molecules by pancreatic elastase using HS-AFM across distinct conformational states.
  • Coiled-coil kinking directs elastase cleavage specifically to the central hinge site, reliably generating the elastase 8 (E8) fragment carrying the integrin binding site.
  • Extended coiled-coil conformations lack targeted cleavage and undergo digestion at arbitrary sites, leading to complete coiled-coil degradation.

Cite This Study

Akter et al. (2026) studied this question.

synapsesocial.com/papers/6aa30949ecbae3efcb7f3af6https://doi.org/10.1016/j.jmb.2026.169991
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