Entry Database : PDB / ID : 2v51 Structure visualization Downloads & linksTitle Structure of MAL-RPEL1 complexed to actin ComponentsACTIN, ALPHA SKELETAL MUSCLE MKL/MYOCARDIN-LIKE PROTEIN 1 DetailsKeywords STRUCTURAL PROTEIN/CONTRACTILE PROTEIN / STRUCTURAL PROTEIN-CONTRACTILE PROTEIN COMPLEX / CONTRACTILE PROTEIN / STRUCTURAL PROTEIN / NUCLEOTIDE-BINDING / TRANSCRIPTION REGULATION / TRANSCRIPTION / PHOSPHOPROTEIN / MUSCLE PROTEIN / METHYLATION / ATP-BINDING / CYTOSKELETON / MAL / RPEL / ACTIN / NUCLEUSFunction / homology Function and homology informationFunction Domain/homology Component
SUMOylation of transcription cofactors / RHO GTPases Activate Formins / smooth muscle cell differentiation / cytoskeletal motor activator activity / tropomyosin binding / mesenchyme migration / troponin I binding / myosin heavy chain binding / filamentous actin / actin filament bundle ... SUMOylation of transcription cofactors / RHO GTPases Activate Formins / smooth muscle cell differentiation / cytoskeletal motor activator activity / tropomyosin binding / mesenchyme migration / 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 / negative regulation of apoptotic signaling pathway / skeletal muscle myofibril / actin monomer binding / skeletal muscle fiber development / stress fiber / titin binding / forebrain development / actin filament polymerization / filopodium / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / neuron migration / calcium-dependent protein binding / neuron projection development / lamellipodium / actin binding / cell body / actin cytoskeleton organization / transcription coactivator activity / transcription cis-regulatory region binding / molecular adaptor activity / hydrolase activity / protein domain specific binding / DNA-binding transcription factor activity / calcium ion binding / regulation of transcription by RNA polymerase II / positive regulation of gene expression / positive regulation of DNA-templated transcription / magnesium ion binding / positive regulation of transcription by RNA polymerase II / ATP binding / identical protein binding / nucleus / cytoplasm Similarity search - Function Myocardin-like / RPEL repeat / RPEL repeat / RPEL repeat profile. / Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2 / SAP domain superfamily / SAP domain / SAP motif profile. / Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation / SAP domain ... Myocardin-like / RPEL repeat / RPEL repeat / RPEL repeat profile. / Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2 / SAP domain superfamily / SAP domain / SAP motif profile. / Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation / SAP domain / 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 / ATPase, nucleotide binding domain / Nucleotidyltransferase; domain 5 / Alpha-Beta Complex / 2-Layer Sandwich / Alpha Beta Similarity search - Domain/homology ADENOSINE-5'-TRIPHOSPHATE / LATRUNCULIN B / DI(HYDROXYETHYL)ETHER / THIOCYANATE ION / Actin, alpha skeletal muscle / Myocardin-related transcription factor A Similarity search - ComponentBiological species ORYCTOLAGUS CUNICULUS (rabbit)MUS MUSCULUS (house mouse)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 2.35 Å DetailsAuthors Mouilleron, S. / Guettler, S. / Langer, C.A. / Treisman, R. / McDonald, N.Q. CitationJournal : EMBO J. / Year : 2008Title : Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL.Authors : Mouilleron, S. / Guettler, S. / Langer, C.A. / Treisman, R. / McDonald, N.Q. History Deposition Oct 1, 2008 Deposition site : PDBE / Processing site : PDBERevision 1.0 Nov 25, 2008 Provider : repository / Type : Initial releaseRevision 1.1 Jul 13, 2011 Group : Advisory / Version format complianceRevision 1.2 Feb 28, 2018 Group : Database references / Structure summary / Category : audit_author / citation / citation_authorItem : _audit_author.name / _citation.journal_abbrev ... _audit_author.name / _citation.journal_abbrev / _citation.journal_id_ISSN / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _citation_author.name Revision 1.3 May 8, 2024 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Other Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_struct_conn_angle / struct_conn Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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.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_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _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.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
Show all Show less Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.