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Updated: Jul 9, 2026

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
Published on: September 28, 2020
Crystal structure of the human laminin receptor precursor
Kelly V Jamieson1, Jinhua Wu2, Stevan R Hubbard2
1Gene Therapy Center, Cancer Institute and Department of Pathology, New York University School of Medicine, New York, New York 10016.
Abstract:
The human laminin receptor (LamR) interacts with many ligands, including laminin, prions, Sindbis virus, and the polyphenol (-)-epigallocatechin-3-gallate (EGCG), and has been implicated in a number of diseases. LamR is overexpressed on tumor cells, and targeting LamR elicits anti-cancer effects. Here, we report the crystal structure of human LamR, which provides insights into its function and should facilitate the design of novel therapeutics targeting LamR.
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