3BCH
Crystal Structure of the Human Laminin Receptor Precursor
Summary for 3BCH
Entry DOI | 10.2210/pdb3bch/pdb |
Descriptor | 40S ribosomal protein SA (2 entities in total) |
Functional Keywords | laminin receptor, p40 ribosomal protein, acetylation, cytoplasm, phosphorylation, polymorphism, ribonucleoprotein, cell adhesion, ribosomal protein |
Biological source | Homo sapiens (human) |
Cellular location | Cell membrane: P08865 |
Total number of polymer chains | 1 |
Total formula weight | 28205.04 |
Authors | Jamieson, K.V.,Wu, J.,Hubbard, S.R.,Meruelo, D. (deposition date: 2007-11-12, release date: 2007-12-04, Last modification date: 2024-02-21) |
Primary citation | Jamieson, K.V.,Wu, J.,Hubbard, S.R.,Meruelo, D. Crystal structure of the human laminin receptor precursor. J.Biol.Chem., 283:3002-3005, 2008 Cited by PubMed 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. PubMed: 18063583DOI: 10.1074/jbc.C700206200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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