3LK3
Crystal structure of CapZ bound to the CPI and CSI uncapping motifs from CARMIL
Summary for 3LK3
Entry DOI | 10.2210/pdb3lk3/pdb |
Related | 3LK2 3LK4 |
Descriptor | F-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 Keywords | capz, carmil, actin filaments, uncapping, actin-filament regulators, protein-protein complex, actin capping, actin-binding, cytoplasm, cytoskeleton, protein binding |
Biological source | Gallus gallus (chicken) More |
Total number of polymer chains | 3 |
Total formula weight | 77389.83 |
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 citation | Hernandez-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: 20357771DOI: 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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