Entry | Database: PDB / ID: 8uf4 |
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Title | Crystal structure of wildtype dystroglycan proteolytic domain (juxtamembrane domain) |
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Components | - Beta-dystroglycan
- a-dystroglycan
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Keywords | CELL ADHESION / SEA domain / mechanoreceptor |
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Function / homology | Function and homology information
Defective POMT2 causes MDDGA2, MDDGB2 and MDDGC2 / Defective POMT1 causes MDDGA1, MDDGB1 and MDDGC1 / muscle attachment / dystroglycan complex / nerve maturation / Defective POMGNT1 causes MDDGA3, MDDGB3 and MDDGC3 / regulation of embryonic cell shape / retrograde trans-synaptic signaling by trans-synaptic protein complex / positive regulation of basement membrane assembly involved in embryonic body morphogenesis / O-linked glycosylation ...Defective POMT2 causes MDDGA2, MDDGB2 and MDDGC2 / Defective POMT1 causes MDDGA1, MDDGB1 and MDDGC1 / muscle attachment / dystroglycan complex / nerve maturation / Defective POMGNT1 causes MDDGA3, MDDGB3 and MDDGC3 / regulation of embryonic cell shape / retrograde trans-synaptic signaling by trans-synaptic protein complex / positive regulation of basement membrane assembly involved in embryonic body morphogenesis / O-linked glycosylation / contractile ring / regulation of gastrulation / calcium-dependent cell-matrix adhesion / morphogenesis of an epithelial sheet / dystrophin-associated glycoprotein complex / microtubule anchoring / laminin-1 binding / response to denervation involved in regulation of muscle adaptation / positive regulation of myelination / basement membrane organization / photoreceptor ribbon synapse / nerve development / dystroglycan binding / cellular response to cholesterol / Formation of the dystrophin-glycoprotein complex (DGC) / vinculin binding / regulation of epithelial to mesenchymal transition / EGR2 and SOX10-mediated initiation of Schwann cell myelination / myelination in peripheral nervous system / branching involved in salivary gland morphogenesis / skeletal muscle tissue regeneration / costamere / commissural neuron axon guidance / node of Ranvier / angiogenesis involved in wound healing / axon regeneration / structural constituent of muscle / positive regulation of cell-matrix adhesion / regulation of neurotransmitter receptor localization to postsynaptic specialization membrane / response to muscle activity / epithelial tube branching involved in lung morphogenesis / regulation of synapse organization / alpha-actinin binding / membrane protein ectodomain proteolysis / basement membrane / positive regulation of oligodendrocyte differentiation / Non-integrin membrane-ECM interactions / postsynaptic cytosol / plasma membrane raft / ECM proteoglycans / negative regulation of MAPK cascade / heart morphogenesis / laminin binding / tubulin binding / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / SH2 domain binding / nuclear periphery / axon guidance / negative regulation of cell migration / morphogenesis of an epithelium / GABA-ergic synapse / filopodium / adherens junction / sarcolemma / regulation of synaptic plasticity / response to peptide hormone / Golgi lumen / Regulation of expression of SLITs and ROBOs / cellular response to mechanical stimulus / protein transport / lamellipodium / actin binding / virus receptor activity / : / basolateral plasma membrane / postsynaptic membrane / cytoskeleton / endoplasmic reticulum lumen / external side of plasma membrane / focal adhesion / intracellular membrane-bounded organelle / calcium ion binding / protein-containing complex binding / glutamatergic synapse / extracellular space / extracellular exosome / extracellular region / nucleoplasm / membrane / plasma membrane / cytosol / cytoplasmSimilarity search - Function Dystroglycan-type cadherin-like / Dystroglycan, C-terminal / Alpha-dystroglycan domain 2 / DG-type SEA domain / Alpha-dystroglycan N-terminal domain 2 / Dystroglycan (Dystrophin-associated glycoprotein 1) / Alpha-Dystroglycan N-terminal domain 2 / DG-type SEA domain profile. / Dystroglycan-type cadherin-like domains. / Putative Ig domain ...Dystroglycan-type cadherin-like / Dystroglycan, C-terminal / Alpha-dystroglycan domain 2 / DG-type SEA domain / Alpha-dystroglycan N-terminal domain 2 / Dystroglycan (Dystrophin-associated glycoprotein 1) / Alpha-Dystroglycan N-terminal domain 2 / DG-type SEA domain profile. / Dystroglycan-type cadherin-like domains. / Putative Ig domain / Cadherin-like superfamily / Immunoglobulin-like foldSimilarity search - Domain/homology |
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Biological species | Homo sapiens (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.43 Å |
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Authors | Anderson, M.J.M. / Shi, K. / Hayward, A.N. / Uhlens, C. / Evans III, R.L. / Grant, E. / Greenberg, L. / Aihara, H. / Gordon, W.R. |
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Funding support | United States, 2items Organization | Grant number | Country |
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National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | 5R35GM119483 | United States | National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | 5R35GM118047 | United States |
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Citation | Journal: Structure / Year: 2024 Title: Molecular basis of proteolytic cleavage regulation by the extracellular matrix receptor dystroglycan. Authors: Anderson, M.J.M. / Hayward, A.N. / Smiley, A.T. / Shi, K. / Pawlak, M.R. / Aird, E.J. / Grant, E. / Greenberg, L. / Aihara, H. / Evans 3rd, R.L. / Ulens, C. / Gordon, W.R. |
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History | Deposition | Oct 3, 2023 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Sep 11, 2024 | Provider: repository / Type: Initial release |
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Revision 1.1 | Nov 6, 2024 | Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification |
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Revision 1.2 | Mar 26, 2025 | Group: Database references / Category: citation / citation_author Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year |
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