3IDW: Crystal structure of Sla1 homology domain 2

During clathrin-mediated endocytosis, adaptor proteins play central roles in coordinating the assembly of clathrin coats and cargo selection. Here we characterize the binding of the yeast endocytic adaptor Sla1p to clathrin through a variant clathrin-binding motif that is negatively regulated by the Sla1p SHD2 domain. The crystal structure of SHD2 identifies the domain as a sterile alpha-motif (SAM) domain and shows a propensity to oligomerize. By co-immunoprecipitation, Sla1p binds to clathrin and self-associates in vivo. Mutations in the clathrin-binding motif that abolish clathrin binding and structure-based mutations in SHD2 that impede self-association result in endocytosis defects and altered dynamics of Sla1p assembly at the sites of endocytosis. These results define a novel mechanism for negative regulation of clathrin binding by an adaptor and suggest a role for SAM domains in clathrin-mediated endocytosis.
PDB ID: 3IDWDownload
MMDB ID: 80261
PDB Deposition Date: 2009/7/21
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 1.85  Å
Source Organism:
Similar Structures:
Biological Unit for 3IDW: monomeric; determined by author and by software (PISA)
Molecular Components in 3IDW
Label Count Molecule
Protein (1 molecule)
Actin Cytoskeleton-regulatory Complex Protein Sla1(Gene symbol: SLA1)
Molecule annotation
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Citing MMDB