3ZYL
Structure of a truncated CALM (PICALM) ANTH domain
Summary for 3ZYL
Entry DOI | 10.2210/pdb3zyl/pdb |
Related | 1HF8 1HFA 1HG2 1HG5 3ZYK 3ZYM |
Descriptor | PHOSPHATIDYLINOSITOL-BINDING CLATHRIN ASSEMBLY PROTEIN (2 entities in total) |
Functional Keywords | endocytosis, endobrevin, synaptobrevin, vamp2, vamp3, ap180, plasma membrane, adaptor protein |
Biological source | RATTUS NORVEGICUS (NORWAY RAT) |
Total number of polymer chains | 2 |
Total formula weight | 61791.24 |
Authors | Miller, S.E.,Sahlender, D.A.,Graham, S.C.,Honing, S.,Robinson, M.S.,Peden, A.A.,Owen, D.J. (deposition date: 2011-08-23, release date: 2011-12-07, Last modification date: 2023-12-20) |
Primary citation | Miller, S.E.,Sahlender, D.A.,Graham, S.C.,Honing, S.,Robinson, M.S.,Peden, A.A.,Owen, D.J. The molecular basis for the endocytosis of small R-SNAREs by the clathrin adaptor CALM. Cell, 147:1118-1131, 2011 Cited by PubMed Abstract: SNAREs provide a large part of the specificity and energy needed for membrane fusion and, to do so, must be localized to their correct membranes. Here, we show that the R-SNAREs VAMP8, VAMP3, and VAMP2, which cycle between the plasma membrane and endosomes, bind directly to the ubiquitously expressed, PtdIns4,5P(2)-binding, endocytic clathrin adaptor CALM/PICALM. X-ray crystallography shows that the N-terminal halves of their SNARE motifs bind the CALM(ANTH) domain as helices in a manner that mimics SNARE complex formation. Mutation of residues in the CALM:SNARE interface inhibits binding in vitro and prevents R-SNARE endocytosis in vivo. Thus, CALM:R-SNARE interactions ensure that R-SNAREs, required for the fusion of endocytic clathrin-coated vesicles with endosomes and also for subsequent postendosomal trafficking, are sorted into endocytic vesicles. CALM's role in directing the endocytosis of small R-SNAREs may provide insight into the association of CALM/PICALM mutations with growth retardation, cognitive defects, and Alzheimer's disease. PubMed: 22118466DOI: 10.1016/j.cell.2011.10.038 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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