Entry Database : PDB / ID : 6rsw Structure visualization Downloads & linksTitle HFD domain of mouse CAP1 bound to the pointed end of G-actin ComponentsActin, alpha skeletal muscle Adenylyl cyclase-associated protein 1 Twinfilin-1 DetailsKeywords CONTRACTILE PROTEIN / Actin binding proteinFunction / homology Function and homology informationFunction Domain/homology Component
regulation of actin phosphorylation / ameboidal-type cell migration / RHOBTB2 GTPase cycle / sequestering of actin monomers / negative regulation of actin filament polymerization / actin filament depolymerization / barbed-end actin filament capping / regulation of lamellipodium assembly / cytoskeletal motor activator activity / cortical actin cytoskeleton ... regulation of actin phosphorylation / ameboidal-type cell migration / RHOBTB2 GTPase cycle / sequestering of actin monomers / negative regulation of actin filament polymerization / actin filament depolymerization / barbed-end actin filament capping / regulation of lamellipodium assembly / cytoskeletal motor activator activity / cortical actin cytoskeleton / myofibril / tropomyosin binding / mesenchyme migration / positive regulation of cardiac muscle hypertrophy / troponin I binding / myosin heavy chain binding / filamentous actin / actin filament bundle / skeletal muscle thin filament assembly / striated muscle thin filament / actin filament bundle assembly / adenylate cyclase binding / skeletal muscle myofibril / actin monomer binding / skeletal muscle fiber development / stress fiber / titin binding / phosphatidylinositol-4,5-bisphosphate binding / actin filament polymerization / Neutrophil degranulation / cAMP-mediated signaling / receptor-mediated endocytosis / filopodium / actin filament / actin filament organization / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / cell morphogenesis / positive regulation of neuron projection development / calcium-dependent protein binding / cell-cell junction / actin filament binding / actin cytoskeleton / lamellipodium / actin binding / cell body / actin cytoskeleton organization / protein tyrosine kinase activity / hydrolase activity / protein domain specific binding / calcium ion binding / protein-containing complex binding / positive regulation of gene expression / perinuclear region of cytoplasm / magnesium ion binding / extracellular region / ATP binding / identical protein binding / plasma membrane / cytoplasm / cytosol Similarity search - Function Adenylate cyclase-associated CAP, N-terminal domain / Adenylate cyclase-associated CAP, N-terminal / CAP, conserved site, N-terminal / CAP, conserved site, C-terminal / Adenylate cyclase-associated CAP, N-terminal domain superfamily / CAP N-terminal conserved motif / CAP protein signature 1. / CAP protein signature 2. / Adenylate cyclase-associated CAP / Adenylate cyclase-associated CAP, C-terminal ... Adenylate cyclase-associated CAP, N-terminal domain / Adenylate cyclase-associated CAP, N-terminal / CAP, conserved site, N-terminal / CAP, conserved site, C-terminal / Adenylate cyclase-associated CAP, N-terminal domain superfamily / CAP N-terminal conserved motif / CAP protein signature 1. / CAP protein signature 2. / Adenylate cyclase-associated CAP / Adenylate cyclase-associated CAP, C-terminal / Adenylate cyclase associated (CAP) C terminal / Adenylate cyclase-associated CAP, C-terminal superfamily / CARP motif / Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product. / C-CAP/cofactor C-like domain / Twinfilin / C-CAP/cofactor C-like domain profile. / Cyclase-associated protein CAP/septum formation inhibitor MinC, C-terminal / Actin; Chain A, domain 2 / Actin; Chain A, domain 2 / Actin-depolymerising factor homology domain / Cofilin/tropomyosin-type actin-binding protein / ADF-H domain profile. / Actin depolymerisation factor/cofilin -like domains / Severin / Severin / ADF-H/Gelsolin-like domain superfamily / ATPase, substrate binding domain, subdomain 4 / Actin; Chain A, domain 4 / ATPase, nucleotide binding domain / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / ATPase, nucleotide binding domain / Alpha Horseshoe / Nucleotidyltransferase; domain 5 / Roll / Alpha-Beta Complex / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta Similarity search - Domain/homologyBiological species Mus musculus (house mouse)Oryctolagus cuniculus (rabbit)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.95 Å DetailsAuthors Kotila, T. / Kogan, K. / Lappalainen, P. Funding support Finland, 2items Details Hide detailsOrganization Grant number Country Academy of Finland 320161 Finland Academy of Finland 307415 Finland
CitationJournal : Nat Commun / Year : 2019Title : Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin.Authors : Kotila, T. / Wioland, H. / Enkavi, G. / Kogan, K. / Vattulainen, I. / Jegou, A. / Romet-Lemonne, G. / Lappalainen, P. History Deposition May 22, 2019 Deposition site : PDBE / Processing site : PDBERevision 1.0 Nov 27, 2019 Provider : repository / Type : Initial releaseRevision 1.1 Dec 4, 2019 Group : Database references / Category : citationItem : _citation.journal_volume / _citation.page_first ... _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title Revision 1.2 Jan 24, 2024 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Refinement description Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / refine / struct_conn Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _refine.pdbx_diffrn_id / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id
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