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3ZYL

Structure of a truncated CALM (PICALM) ANTH domain

Summary for 3ZYL
Entry DOI10.2210/pdb3zyl/pdb
Related1HF8 1HFA 1HG2 1HG5 3ZYK 3ZYM
DescriptorPHOSPHATIDYLINOSITOL-BINDING CLATHRIN ASSEMBLY PROTEIN (2 entities in total)
Functional Keywordsendocytosis, endobrevin, synaptobrevin, vamp2, vamp3, ap180, plasma membrane, adaptor protein
Biological sourceRATTUS NORVEGICUS (NORWAY RAT)
Total number of polymer chains2
Total formula weight61791.24
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 citationMiller, 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: 22118466
DOI: 10.1016/j.cell.2011.10.038
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

226707

數據於2024-10-30公開中

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