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- SASDAT6: Integrin beta4, fragment of the cytoplasmic region encompassing t... -

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Basic information

Entry
Database: SASBDB / ID: SASDAT6
SampleIntegrin beta4, fragment of the cytoplasmic region encompassing the third and fourth FnIII domains
  • Integrin beta-4 (protein), Homo sapiens
Function / homology
Function and homology information


trophoblast cell migration / Type I hemidesmosome assembly / hemidesmosome assembly / nail development / hemidesmosome / peripheral nervous system myelin formation / skin morphogenesis / Laminin interactions / mesodermal cell differentiation / filopodium assembly ...trophoblast cell migration / Type I hemidesmosome assembly / hemidesmosome assembly / nail development / hemidesmosome / peripheral nervous system myelin formation / skin morphogenesis / Laminin interactions / mesodermal cell differentiation / filopodium assembly / Differentiation of keratinocytes in interfollicular epidermis in mammalian skin / integrin complex / Assembly of collagen fibrils and other multimeric structures / Syndecan interactions / cell leading edge / basement membrane / cell-matrix adhesion / basal plasma membrane / integrin-mediated signaling pathway / cell motility / G protein-coupled receptor binding / cell-cell adhesion / response to wounding / autophagy / integrin binding / cell junction / nuclear membrane / receptor complex / cell adhesion / focal adhesion / nucleolus / cell surface / extracellular exosome / metal ion binding / plasma membrane
Similarity search - Function
Integrin beta-4 subunit / Na-Ca exchanger/integrin-beta4 / Calx-beta domain / Domains in Na-Ca exchangers and integrin-beta4 / CalX-like domain superfamily / Integrin beta, epidermal growth factor-like domain 1 / Integrin beta epidermal growth factor like domain 1 / Integrin beta tail domain / Integrin beta subunit, tail / Integrin beta tail domain superfamily ...Integrin beta-4 subunit / Na-Ca exchanger/integrin-beta4 / Calx-beta domain / Domains in Na-Ca exchangers and integrin-beta4 / CalX-like domain superfamily / Integrin beta, epidermal growth factor-like domain 1 / Integrin beta epidermal growth factor like domain 1 / Integrin beta tail domain / Integrin beta subunit, tail / Integrin beta tail domain superfamily / Integrin_B_tail / Integrin beta subunit, VWA domain / Integrin beta subunit / Integrin beta N-terminal / Integrin beta chain VWA domain / Integrin plexin domain / Integrins beta chain cysteine-rich domain signature. / Integrin beta subunits (N-terminal portion of extracellular region) / EGF-like domain, extracellular / EGF-like domain / PSI domain / domain found in Plexins, Semaphorins and Integrins / von Willebrand factor A-like domain superfamily / EGF-like domain signature 2. / EGF-like domain signature 1. / Fibronectin type III domain / EGF-like domain / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
CitationJournal: Acta Crystallogr D Biol Crystallogr / Year: 2015
Title: Combination of X-ray crystallography, SAXS and DEER to obtain the structure of the FnIII-3,4 domains of integrin α6β4.
Authors: Noelia Alonso-García / Inés García-Rubio / José A Manso / Rubén M Buey / Hector Urien / Arnoud Sonnenberg / Gunnar Jeschke / José M de Pereda /
Abstract: Integrin α6β4 is a major component of hemidesmosomes that mediate the stable anchorage of epithelial cells to the underlying basement membrane. Integrin α6β4 has also been implicated in cell ...Integrin α6β4 is a major component of hemidesmosomes that mediate the stable anchorage of epithelial cells to the underlying basement membrane. Integrin α6β4 has also been implicated in cell proliferation and migration and in carcinoma progression. The third and fourth fibronectin type III domains (FnIII-3,4) of integrin β4 mediate binding to the hemidesmosomal proteins BPAG1e and BPAG2, and participate in signalling. Here, it is demonstrated that X-ray crystallography, small-angle X-ray scattering and double electron-electron resonance (DEER) complement each other to solve the structure of the FnIII-3,4 region. The crystal structures of the individual FnIII-3 and FnIII-4 domains were solved and the relative arrangement of the FnIII domains was elucidated by combining DEER with site-directed spin labelling. Multiple structures of the interdomain linker were modelled by Monte Carlo methods complying with DEER constraints, and the final structures were selected against experimental scattering data. FnIII-3,4 has a compact and cambered flat structure with an evolutionary conserved surface that is likely to correspond to a protein-interaction site. Finally, this hybrid method is of general application for the study of other macromolecules and complexes.
Contact author
  • Jose M de Pereda (USAL, La Universidad de Salamanca, Salamanca, Spain)

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Structure visualization

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Models

Model #219
Type: dummy / Software: DAMMIF / Radius of dummy atoms: 1.50 A / Chi-square value: 1.976836
Search similar-shape structures of this assembly by Omokage search (details)
Model #220
Type: atomic / Software: CRYSOL / Chi-square value: 1.297321
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Integrin beta4, fragment of the cytoplasmic region encompassing the third and fourth FnIII domains
Specimen concentration: 1.50-48.60
BufferName: Sodium Phosphate / Concentration: 20.00 mM / pH: 7.5 / Composition: 150 mM NaCl, 5% glycerol, 3 mM DTT
Entity #133Type: protein / Description: Integrin beta-4 / Formula weight: 23.359 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P16144
Sequence: GSHMVPDTPT RLVFSALGPT SLRVSWQEPR CERPLQGYSV EYQLLNGGEL HRLNIPNPAQ TSVVVEDLLP NHSYVFRVRA QSQEGWGRER EGVITIESQV HPQSPLCPLP GSAFTLSTPS APGPLVFTAL SPDSLQLSWE RPRRPNGDIV GYLVTCEMAQ GGGPATAFRV ...Sequence:
GSHMVPDTPT RLVFSALGPT SLRVSWQEPR CERPLQGYSV EYQLLNGGEL HRLNIPNPAQ TSVVVEDLLP NHSYVFRVRA QSQEGWGRER EGVITIESQV HPQSPLCPLP GSAFTLSTPS APGPLVFTAL SPDSLQLSWE RPRRPNGDIV GYLVTCEMAQ GGGPATAFRV DGDSPESRLT VPGLSENVPY KFKVQARTTE GFGPEREGII TIES

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Experimental information

BeamInstrument name: PETRA III P12 / City: Hamburg / : Germany / Type of source: X-ray synchrotron / Wavelength: 0.12 Å / Dist. spec. to detc.: 3.1 mm
DetectorName: Pilatus 2M
Scan
Measurement date: Aug 6, 2013 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 0.05 sec. / Number of frames: 20 / Unit: 1/nm /
MinMax
Q0.0576 3.4909
Distance distribution function P(R)
Sofotware P(R): GNOM 4.6 / Number of points: 494 /
MinMax
Q0.05955 3.013
P(R) point1 494
R0 7
Result
D max: 7 / Type of curve: extrapolated
Comments: Combined use of SAXS, crystal structures, site directed spin labeling, double electron-electron resonance (DEER), and molecular modeling to analyze the structure of FnIII-3,4.
ExperimentalStandardPorod
MW19.2 kDa19.2 kDa20 kDa
Volume--32 nm3

P(R)Guinier
Forward scattering, I0586 590
Radius of gyration, Rg2.2 nm2.2 nm

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