Entry Database : PDB / ID : 6ghd Structure visualization Downloads & linksTitle Structural analysis of the ternary complex between lamin A/C, BAF and emerin identifies an interface disrupted in autosomal recessive progeroid diseases ComponentsBarrier-to-autointegration factor Emerin Prelamin-A/C DetailsKeywords PROTEIN BINDING / nuclear envelope / gene expression / ternary complexFunction / homology Function and homology informationFunction Domain/homology Component
TMEM240-body / nuclear membrane organization / structural constituent of nuclear lamina / negative regulation of mesenchymal cell proliferation / negative regulation of protein ADP-ribosylation / establishment or maintenance of microtubule cytoskeleton polarity / ventricular cardiac muscle cell development / Breakdown of the nuclear lamina / DNA double-strand break attachment to nuclear envelope / Depolymerization of the Nuclear Lamina ... TMEM240-body / nuclear membrane organization / structural constituent of nuclear lamina / negative regulation of mesenchymal cell proliferation / negative regulation of protein ADP-ribosylation / establishment or maintenance of microtubule cytoskeleton polarity / ventricular cardiac muscle cell development / Breakdown of the nuclear lamina / DNA double-strand break attachment to nuclear envelope / Depolymerization of the Nuclear Lamina / Nuclear Envelope Breakdown / nuclear envelope organization / nuclear pore localization / lamin filament / protein localization to nuclear envelope / mitotic nuclear membrane reassembly / nuclear lamina / XBP1(S) activates chaperone genes / Initiation of Nuclear Envelope (NE) Reformation / regulation of protein localization to nucleus / RHOD GTPase cycle / nuclear outer membrane / regulation of canonical Wnt signaling pathway / nuclear migration / regulation of telomere maintenance / negative regulation of cardiac muscle hypertrophy in response to stress / nuclear inner membrane / muscle organ development / Integration of viral DNA into host genomic DNA / Autointegration results in viral DNA circles / negative regulation of type I interferon production / intermediate filament / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / negative regulation of viral genome replication / Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models / negative regulation of cGAS/STING signaling pathway / 2-LTR circle formation / beta-tubulin binding / negative regulation of release of cytochrome c from mitochondria / Vpr-mediated nuclear import of PICs / skeletal muscle cell differentiation / Integration of provirus / APOBEC3G mediated resistance to HIV-1 infection / protein localization to nucleus / RHOG GTPase cycle / chromosome organization / RAC2 GTPase cycle / RAC3 GTPase cycle / heterochromatin formation / negative regulation of fibroblast proliferation / condensed chromosome / regulation of cell migration / RAC1 GTPase cycle / Meiotic synapsis / negative regulation of innate immune response / positive regulation of protein export from nucleus / muscle contraction / negative regulation of extrinsic apoptotic signaling pathway / response to virus / regulation of protein stability / negative regulation of canonical Wnt signaling pathway / protein localization / structural constituent of cytoskeleton / cellular response to growth factor stimulus / nuclear matrix / DNA integration / spindle / protein import into nucleus / cellular senescence / Signaling by BRAF and RAF1 fusions / chromatin organization / nuclear envelope / site of double-strand break / actin binding / cellular response to hypoxia / double-stranded DNA binding / nuclear membrane / microtubule / response to oxidative stress / nuclear speck / cadherin binding / negative regulation of cell population proliferation / positive regulation of gene expression / chromatin / structural molecule activity / perinuclear region of cytoplasm / endoplasmic reticulum / protein homodimerization activity / DNA binding / nucleoplasm / identical protein binding / membrane / nucleus / cytoplasm / cytosol Similarity search - Function Emerin, LEM domain / Emerin / Transcription Termination Factor Rho, Rna-binding Domain; Chain A, Domain 1 - #40 / Barrier-to-autointegration factor, BAF / Lamin Tail domain / Barrier- to-autointegration factor, BAF / Barrier-to-autointegration factor, BAF superfamily / Barrier to autointegration factor / Barrier to autointegration factor / Lamin tail domain superfamily ... Emerin, LEM domain / Emerin / Transcription Termination Factor Rho, Rna-binding Domain; Chain A, Domain 1 - #40 / Barrier-to-autointegration factor, BAF / Lamin Tail domain / Barrier- to-autointegration factor, BAF / Barrier-to-autointegration factor, BAF superfamily / Barrier to autointegration factor / Barrier to autointegration factor / Lamin tail domain superfamily / Lamin tail domain / Lamin Tail Domain / Lamin-tail (LTD) domain profile. / LEM domain / LEM domain / LEM domain profile. / in nuclear membrane-associated proteins / LEM/LEM-like domain superfamily / Transcription Termination Factor Rho, Rna-binding Domain; Chain A, Domain 1 / Intermediate filament protein, conserved site / Intermediate filament protein / Intermediate filament (IF) rod domain signature. / Intermediate filament, rod domain / Intermediate filament (IF) rod domain profile. / Intermediate filament protein / DNA polymerase; domain 1 / Immunoglobulin-like / Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha Similarity search - Domain/homologyBiological species Homo sapiens (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 2.1 Å DetailsAuthors Samson, C. / Petitalot, A. / Celli, F. / Herrada, I. / Ropars, V. / Ledu, M.H. / Nhiri, N. / Arteni, A.A. / Buendia, B. / ZinnJustin, S. CitationJournal : Nucleic Acids Res. / Year : 2018Title : Structural analysis of the ternary complex between lamin A/C, BAF and emerin identifies an interface disrupted in autosomal recessive progeroid diseases.Authors : Samson, C. / Petitalot, A. / Celli, F. / Herrada, I. / Ropars, V. / Le Du, M.H. / Nhiri, N. / Jacquet, E. / Arteni, A.A. / Buendia, B. / Zinn-Justin, S. History Deposition May 7, 2018 Deposition site : PDBE / Processing site : PDBERevision 1.0 Aug 8, 2018 Provider : repository / Type : Initial releaseRevision 1.1 Aug 29, 2018 Group : Data collection / Database references / Category : citation / Item : _citation.pdbx_database_id_DOIRevision 1.2 Nov 14, 2018 Group : Data collection / Database references / Category : citation / citation_author / pdbx_database_procItem : _citation.journal_volume / _citation.page_first ... _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title Revision 1.3 Jan 17, 2024 Group : Data collection / Database references / Refinement descriptionCategory : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
Show all Show less