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.
Jamieson
Kelly V
KV
Gene Therapy Center, Cancer Institute and Department of Pathology, New York University School of Medicine, New York, New York 10016.
Wu
Jinhua
J
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.
Hubbard
Stevan R
SR
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.
Meruelo
Daniel
D
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.
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