Crystal structure of the human laminin receptor precursor.
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.
Gene Therapy Center, Cancer Institute and Department of Pathology, New York University School of Medicine, New York, New York 10016.
Kelly V
KV
Jamieson
Structural Biology Program, Kimmel Center for Biology and Medicine of the Skirball Institute, and Department of Pharmacology, New York University School of Medicine, New York, New York 10016.
Jinhua
J
Wu
Structural Biology Program, Kimmel Center for Biology and Medicine of the Skirball Institute, and Department of Pharmacology, New York University School of Medicine, New York, New York 10016. Electronic address: hubbard@saturn.med.nyu.edu.
Stevan R
SR
Hubbard
Gene Therapy Center, Cancer Institute and Department of Pathology, New York University School of Medicine, New York, New York 10016. Electronic address: daniel.meruelo@med.nyu.edu.
Daniel
D
Meruelo
D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans; D018360:Crystallography, X-Ray; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D011485:Protein Binding; D011498:Protein Precursors / Q000737:chemistry*; D011956:Receptors, Cell Surface / Q000737:chemistry; D017474:Receptors, Laminin / Q000737:chemistry*; D012441:Saccharomyces cerevisiae; D017386:Sequence Homology, Amino Acid
D008024:Ligands; D011498:Protein Precursors; D011956:Receptors, Cell Surface; D017474:Receptors, Laminin