5GV0
Crystal structure of the membrane-proximal domain of mouse lysosome-associated membrane protein 1 (LAMP-1)
Summary for 5GV0
Entry DOI | 10.2210/pdb5gv0/pdb |
Related | 5GV3 |
Descriptor | Lysosome-associated membrane glycoprotein 1, SULFATE ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | membrane protein |
Biological source | Mus musculus (Mouse) |
Total number of polymer chains | 1 |
Total formula weight | 19330.57 |
Authors | Tomabechi, Y.,Ehara, H.,Kukimoto-Niino, M.,Shirouzu, M. (deposition date: 2016-09-01, release date: 2016-10-12, Last modification date: 2024-10-16) |
Primary citation | Terasawa, K.,Tomabechi, Y.,Ikeda, M.,Ehara, H.,Kukimoto-Niino, M.,Wakiyama, M.,Podyma-Inoue, K.A.,Rajapakshe, A.R.,Watabe, T.,Shirouzu, M.,Hara-Yokoyama, M. Lysosome-associated membrane proteins-1 and -2 (LAMP-1 and LAMP-2) assemble via distinct modes Biochem.Biophys.Res.Commun., 479:489-495, 2016 Cited by PubMed Abstract: Lysosome-associated membrane proteins 1 and 2 (LAMP-1 and LAMP-2) have a large, heavily glycosylated luminal domain composed of two subdomains, and are the most abundant protein components in lysosome membranes. LAMP-1 and LAMP-2 have distinct functions, and the presence of both proteins together is required for the essential regulation of autophagy to avoid embryonic lethality. However, the structural aspects of LAMP-1 and LAMP-2 have not been elucidated. In the present study, we demonstrated that the subdomains of LAMP-1 and LAMP-2 adopt the unique β-prism fold, similar to the domain structure of the dendritic cell-specific-LAMP (DC-LAMP, LAMP-3), confirming the conserved aspect of this family of lysosome-associated membrane proteins. Furthermore, we evaluated the effects of the N-domain truncation of LAMP-1 or LAMP-2 on the assembly of LAMPs, based on immunoprecipitation experiments. We found that the N-domain of LAMP-1 is necessary, whereas that of LAMP-2 is repressive, for the organization of a multimeric assembly of LAMPs. Accordingly, the present study suggests for the first time that the assembly modes of LAMP-1 and LAMP-2 are different, which may underlie their distinct functions. PubMed: 27663661DOI: 10.1016/j.bbrc.2016.09.093 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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