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3LK3

Crystal structure of CapZ bound to the CPI and CSI uncapping motifs from CARMIL

Summary for 3LK3
Entry DOI10.2210/pdb3lk3/pdb
Related3LK2 3LK4
DescriptorF-actin-capping protein subunit alpha-1, F-actin-capping protein subunit beta isoforms 1 and 2, Leucine-rich repeat-containing protein 16A, ... (4 entities in total)
Functional Keywordscapz, carmil, actin filaments, uncapping, actin-filament regulators, protein-protein complex, actin capping, actin-binding, cytoplasm, cytoskeleton, protein binding
Biological sourceGallus gallus (chicken)
More
Total number of polymer chains3
Total formula weight77389.83
Authors
Hernandez-Valladares, M.,Kim, T.,Kannan, B.,Tung, A.,Cooper, J.A.,Robinson, R.C. (deposition date: 2010-01-27, release date: 2010-04-07, Last modification date: 2023-11-01)
Primary citationHernandez-Valladares, M.,Kim, T.,Kannan, B.,Tung, A.,Aguda, A.H.,Larsson, M.,Cooper, J.A.,Robinson, R.C.
Structural characterization of a capping protein interaction motif defines a family of actin filament regulators.
Nat.Struct.Mol.Biol., 17:497-503, 2010
Cited by
PubMed Abstract: Capping protein (CP) regulates actin dynamics by binding the barbed ends of actin filaments. Removal of CP may be one means to harness actin polymerization for processes such as cell movement and endocytosis. Here we structurally and biochemically investigated a CP interaction (CPI) motif present in the otherwise unrelated proteins CARMIL and CD2AP. The CPI motif wraps around the stalk of the mushroom-shaped CP at a site distant from the actin-binding interface, which lies on the top of the mushroom cap. We propose that the CPI motif may act as an allosteric modulator, restricting CP to a low-affinity, filament-binding conformation. Structure-based sequence alignments extend the CPI motif-containing family to include CIN85, CKIP-1, CapZIP and a relatively uncharacterized protein, WASHCAP (FAM21). Peptides comprising these CPI motifs are able to inhibit CP and to uncap CP-bound actin filaments.
PubMed: 20357771
DOI: 10.1038/nsmb.1792
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.68 Å)
Structure validation

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