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6gvk
From Proteopedia
(Difference between revisions)
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<StructureSection load='6gvk' size='340' side='right'caption='[[6gvk]], [[Resolution|resolution]] 1.55Å' scene=''> | <StructureSection load='6gvk' size='340' side='right'caption='[[6gvk]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6gvk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GVK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6gvk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GVK FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[ | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6gvl|6gvl]]</td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ITGB4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gvk OCA], [http://pdbe.org/6gvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gvk RCSB], [http://www.ebi.ac.uk/pdbsum/6gvk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gvk ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gvk OCA], [http://pdbe.org/6gvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gvk RCSB], [http://www.ebi.ac.uk/pdbsum/6gvk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gvk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ITB4_HUMAN ITB4_HUMAN]] Integrin alpha-6/beta-4 is a receptor for laminin. Plays a critical structural role in the hemidesmosome of epithelial cells. Is required for the regulation of keratinocyte polarity and motility.<ref>PMID:12482924</ref> <ref>PMID:19403692</ref> [[http://www.uniprot.org/uniprot/DYST_HUMAN DYST_HUMAN]] Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1 (By similarity).[UniProtKB:Q91ZU6] Isoform 3: plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity. Isoform 6: required for bundling actin filaments around the nucleus.<ref>PMID:10428034</ref> <ref>PMID:12482924</ref> <ref>PMID:19403692</ref> Isoform 7: regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. | [[http://www.uniprot.org/uniprot/ITB4_HUMAN ITB4_HUMAN]] Integrin alpha-6/beta-4 is a receptor for laminin. Plays a critical structural role in the hemidesmosome of epithelial cells. Is required for the regulation of keratinocyte polarity and motility.<ref>PMID:12482924</ref> <ref>PMID:19403692</ref> [[http://www.uniprot.org/uniprot/DYST_HUMAN DYST_HUMAN]] Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1 (By similarity).[UniProtKB:Q91ZU6] Isoform 3: plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity. Isoform 6: required for bundling actin filaments around the nucleus.<ref>PMID:10428034</ref> <ref>PMID:12482924</ref> <ref>PMID:19403692</ref> Isoform 7: regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Mechanical stability of epithelia requires firm attachment to the basement membrane via hemidesmosomes. Dysfunction of hemidesmosomal proteins causes severe skin-blistering diseases. Two plakins, plectin and BP230 (BPAG1e), link the integrin alpha6beta4 to intermediate filaments in epidermal hemidesmosomes. Here, we show that a linear sequence within the isoform-specific N-terminal region of BP230 binds to the third and fourth FnIII domains of beta4. The crystal structure of the complex and mutagenesis analysis revealed that BP230 binds between the two domains of beta4. BP230 induces closing of the two FnIII domains that are locked in place by an interdomain ionic clasp required for binding. Disruption of BP230-beta4 binding prevents recruitment of BP230 to hemidesmosomes in human keratinocytes, revealing a key role of this interaction for hemidesmosome assembly. Phosphomimetic substitutions in beta4 and BP230 destabilize the complex. Thus, our study provides insights into the architecture of hemidesmosomes and potential mechanisms of regulation. | ||
| + | |||
| + | Integrin alpha6beta4 Recognition of a Linear Motif of Bullous Pemphigoid Antigen BP230 Controls Its Recruitment to Hemidesmosomes.,Manso JA, Gomez-Hernandez M, Carabias A, Alonso-Garcia N, Garcia-Rubio I, Kreft M, Sonnenberg A, de Pereda JM Structure. 2019 Apr 4. pii: S0969-2126(19)30094-2. doi:, 10.1016/j.str.2019.03.016. PMID:31006587<ref>PMID:31006587</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6gvk" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Alonso-Garcia, N]] | [[Category: Alonso-Garcia, N]] | ||
Revision as of 09:12, 1 May 2019
Second pair of Fibronectin type III domains of integrin beta4 (T1663R mutant) bound to the bullous pemphigoid antigen BP230 (BPAG1e)
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