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- EMDB-27542: Cryo-EM reveals the molecular basis of laminin polymerization and... -
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Open data
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Basic information
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Title | Cryo-EM reveals the molecular basis of laminin polymerization and LN-lamininopathies | |||||||||
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![]() | Laminin / Complex / Basement membrane / STRUCTURAL PROTEIN | |||||||||
Function / homology | ![]() laminin-3 complex / laminin-11 complex / laminin-2 complex / neuronal-glial interaction involved in cerebral cortex radial glia guided migration / laminin-8 complex / laminin complex / laminin-1 complex / laminin-10 complex / retinal blood vessel morphogenesis / regulation of basement membrane organization ...laminin-3 complex / laminin-11 complex / laminin-2 complex / neuronal-glial interaction involved in cerebral cortex radial glia guided migration / laminin-8 complex / laminin complex / laminin-1 complex / laminin-10 complex / retinal blood vessel morphogenesis / regulation of basement membrane organization / L1CAM interactions / morphogenesis of an epithelial sheet / hemidesmosome assembly / glycosphingolipid binding / positive regulation of integrin-mediated signaling pathway / tissue development / Laminin interactions / EGR2 and SOX10-mediated initiation of Schwann cell myelination / endoderm development / branching involved in salivary gland morphogenesis / protein complex involved in cell-matrix adhesion / establishment of epithelial cell apical/basal polarity / camera-type eye development / blood vessel morphogenesis / odontogenesis / MET activates PTK2 signaling / extracellular matrix structural constituent / epithelial tube branching involved in lung morphogenesis / maintenance of blood-brain barrier / positive regulation of muscle cell differentiation / endodermal cell differentiation / regulation of embryonic development / positive regulation of cell adhesion / Non-integrin membrane-ECM interactions / basement membrane / ECM proteoglycans / extracellular matrix disassembly / regulation of cell migration / Degradation of the extracellular matrix / substrate adhesion-dependent cell spreading / extracellular matrix / positive regulation of epithelial cell proliferation / axon guidance / animal organ morphogenesis / Post-translational protein phosphorylation / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / neuron projection development / cell-cell junction / cell migration / retina development in camera-type eye / protein-containing complex assembly / collagen-containing extracellular matrix / cell surface receptor signaling pathway / cell adhesion / positive regulation of cell migration / endoplasmic reticulum lumen / protein phosphorylation / signaling receptor binding / structural molecule activity / perinuclear region of cytoplasm / extracellular space / extracellular exosome / extracellular region / membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||
![]() | Kulczyk AW | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM reveals the molecular basis oflaminin polymerization and LN-lamininopathies. Authors: Arkadiusz W Kulczyk / Karen K McKee / Ximo Zhang / Iwona Bizukojc / Ying Q Yu / Peter D Yurchenco / ![]() Abstract: Laminin polymerization is the major step in basement membranes assembly. Its failures cause laminin N-terminal domain lamininopathies including Pierson syndrome. We have employed cryo-electron ...Laminin polymerization is the major step in basement membranes assembly. Its failures cause laminin N-terminal domain lamininopathies including Pierson syndrome. We have employed cryo-electron microscopy to determine a 3.7 Å structure of the trimeric laminin polymer node containing α1, β1 and γ1 subunits. The structure reveals the molecular basis of calcium-dependent formation of laminin lattice, and provides insights into polymerization defects manifesting in human disease. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 53.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 20 KB 20 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 10.4 KB | Display | ![]() |
Images | ![]() | 26.6 KB | ||
Others | ![]() ![]() ![]() | 50.5 MB 94.9 MB 95.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8dmkMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Unsharpened map | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.972 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: Sharpened map
File | emd_27542_additional_1.map | ||||||||||||
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Annotation | Sharpened map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_27542_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_27542_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Lamimin polymer node
Entire | Name: Lamimin polymer node |
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Components |
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-Supramolecule #1: Lamimin polymer node
Supramolecule | Name: Lamimin polymer node / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 Details: A trimeric complex of the N-terminal fragments (LN, LE1, LE2 domains) from laminin alpha 1, laminin beta 1 and laminin gamma 1. |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 172 KDa |
-Macromolecule #1: Laminin subunit alpha-1
Macromolecule | Name: Laminin subunit alpha-1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 34.709211 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: GLFPAILNLA TNAHISANAT CGEKGPEMFC KLVEHVPGRP VRHAQCRVCD GNSTNPRERH PISHAIDGTN NWWQSPSIQN GREYHWVTV TLDLRQVFQV AYIIIKAANA PRPGNWILER SVDGVKFKPW QYYAVSDTEC LTRYKITPRR GPPTYRADNE V ICTSYYSK ...String: GLFPAILNLA TNAHISANAT CGEKGPEMFC KLVEHVPGRP VRHAQCRVCD GNSTNPRERH PISHAIDGTN NWWQSPSIQN GREYHWVTV TLDLRQVFQV AYIIIKAANA PRPGNWILER SVDGVKFKPW QYYAVSDTEC LTRYKITPRR GPPTYRADNE V ICTSYYSK LVPLEHGEIH TSLINGRPSA DDPSPQLLEF TSARYIRLRL QRIRTLNADL MTLSHRDLRD LDPIVTRRYY YS IKDISVG GMCICYGHAS SCPWDEEAKQ LQCQCEHNTC GESCDRCCPG YHQQPWRPGT ISSGNECE UniProtKB: Laminin subunit alpha-1 |
-Macromolecule #2: Laminin subunit beta-1
Macromolecule | Name: Laminin subunit beta-1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 35.09191 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: GCAEGSCYPA TGDLLIGRAQ KLSVTSTCGL HKPEPYCIVS HLQEDKKCFI CNSQDPYHET LNPDSHLIEN VVTTFAPNRL KIWWQSENG VENVTIQLDL EAEFHFTHLI MTFKTFRPAA MLIERSSDFG KTWGVYRYFA YDCEASFPGI STGPMKKVDD I ICDSRYSD ...String: GCAEGSCYPA TGDLLIGRAQ KLSVTSTCGL HKPEPYCIVS HLQEDKKCFI CNSQDPYHET LNPDSHLIEN VVTTFAPNRL KIWWQSENG VENVTIQLDL EAEFHFTHLI MTFKTFRPAA MLIERSSDFG KTWGVYRYFA YDCEASFPGI STGPMKKVDD I ICDSRYSD IEPSTEGEVI FRALDPAFKI EDPYSPRIQN LLKITNLRIK FVKLHTLGDN LLDSRMEIRE KYYYAVYDMV VR GNCFCYG HASECAPVDG FNEEVEGMVH GHCMCRHNTK GLNCELCMDF YHDLPWRPAE GRNSNACKKC UniProtKB: Laminin subunit beta-1 |
-Macromolecule #3: Laminin subunit gamma-1
Macromolecule | Name: Laminin subunit gamma-1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 34.110816 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MDECTDEGGR PQRCMPEFVN AAFNVTVVAT NTCGTPPEEY CVQTGVTGVT KSCHLCDAGQ PHLQHGAAFL TDYNNQADTT WWQSQTMLA GVQYPSSINL TLHLGKAFDI TYVRLKFHTS RPESFAIYKR TWEDGPWIPY QYYSGSCENT YSKANRGFIR T GGDEQQAL ...String: MDECTDEGGR PQRCMPEFVN AAFNVTVVAT NTCGTPPEEY CVQTGVTGVT KSCHLCDAGQ PHLQHGAAFL TDYNNQADTT WWQSQTMLA GVQYPSSINL TLHLGKAFDI TYVRLKFHTS RPESFAIYKR TWEDGPWIPY QYYSGSCENT YSKANRGFIR T GGDEQQAL CTDEFSDISP LTGGNVAFST LEGRPSAYNF DNSPVLQEWV TATDISVTLN RLNTFGDEVF NDPKVLKSYY YA ISDFAVG GRCKCNGHAS ECMKNEFDKL VCNCKHNTYG VDCEKCLPFF NDRPWRRATA ESASECLP UniProtKB: Laminin subunit gamma-1 |
-Macromolecule #4: 2-acetamido-2-deoxy-beta-D-glucopyranose
Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 4 / Number of copies: 5 / Formula: NAG |
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Molecular weight | Theoretical: 221.208 Da |
Chemical component information | ![]() ChemComp-NAG: |
-Macromolecule #5: CALCIUM ION
Macromolecule | Name: CALCIUM ION / type: ligand / ID: 5 / Number of copies: 1 / Formula: CA |
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Molecular weight | Theoretical: 40.078 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Grid | Model: Quantifoil / Material: GOLD / Mesh: 300 |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Instrument: LEICA EM GP |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 1.8 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 130000 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Protocol: AB INITIO MODEL |
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Output model | ![]() PDB-8dmk: |