4AKM
Crystal structure of the human lysosome-associated membrane protein LAMP-3 (aka DC-LAMP)
Summary for 4AKM
Entry DOI | 10.2210/pdb4akm/pdb |
Descriptor | LYSOSOME-ASSOCIATED MEMBRANE GLYCOPROTEIN 3, IRIDIUM (III) ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | membrane protein, glycosylation, beta prism |
Biological source | HOMO SAPIENS (HUMAN) |
Total number of polymer chains | 2 |
Total formula weight | 38524.70 |
Authors | Krausze, J.,Wilke, S.,Buessow, K. (deposition date: 2012-02-24, release date: 2012-08-15, Last modification date: 2024-10-09) |
Primary citation | Wilke, S.,Krausze, J.,Bussow, K. Crystal Structure of the Conserved Domain of the Dc Lysosomal Associated Membrane Protein: Implications for the Lysosomal Glycocalyx. Bmc Biol., 10:62-, 2012 Cited by PubMed Abstract: The family of lysosome-associated membrane proteins (LAMP) comprises the multifunctional, ubiquitous LAMP-1 and LAMP-2, and the cell type-specific proteins DC-LAMP (LAMP-3), BAD-LAMP (UNC-46, C20orf103) and macrosialin (CD68). LAMPs have been implicated in a multitude of cellular processes, including phagocytosis, autophagy, lipid transport and aging. LAMP-2 isoform A acts as a receptor in chaperone-mediated autophagy. LAMP-2 deficiency causes the fatal Danon disease. The abundant proteins LAMP-1 and LAMP-2 are major constituents of the glycoconjugate coat present on the inside of the lysosomal membrane, the 'lysosomal glycocalyx'. The LAMP family is characterized by a conserved domain of 150 to 200 amino acids with two disulfide bonds. PubMed: 22809326DOI: 10.1186/1741-7007-10-62 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.687 Å) |
Structure validation
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