Difference between revisions of "Frankel:ECM Proteins"

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''<font align="center" font color=#ffffff font size=8>_________ </font>'''''<font color=#000000 font size=8>ECM Proteins</font>'''
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'''<font color=#000000 font size=8>ECM Proteins</font>'''
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''<font align="center" font color=#ffffff font size=8>_______ </font>'''''<font color=#000000 font size=3>Fibronectin</font>'''
  
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'''<font color=#FFFFFF font size=8>HIV-gp160</font>'''
 
 
 
 
[[Image:FN.png|500px]]
 
[[Image:FN.png|500px]]
  
 
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[[Image:GP160_on_mica.png|300px]]
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[[Image:GP160_on_DOPC.png|300px]]
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[[Image:FNselec.png|235px]]
[[Image:Pore50nm.png|300px]]
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[[Image:Pore100nm.png|300px]]
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[[Image:FNseleczoom.png|235px]]
 
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[[Image:FNint.png|500px]]
 
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'''<font color=#045FB4 font size=3> Self assembly and pore formation of HIV gp160 revealed at molecular resolution
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'''<font color=#000000 font size=3> One of the major components of the extracellular matrix (ECM) is fibronectin, this dimeric glycoprotein is involved in numerous cell processes and has important functions in vertebrate development.
 
 
Self assembly of HIV gp160 reconstituted into DOPC bilayer and adsorbed onto mica.
 
  
gp160 forming pore like structures. </font>'''
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Fibronectin in the extracellular matrix interacts with the transmembrane integrins in a highly specific manner. The ECM ligand protein contains a tripeptide recognition site, Arg-Gly-Asp (RGD), responsible for the affinity of the cell surface receptors with its ligand.
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Atomic force microscopy images can be appreciated, these illustrations depict how fibronectin molecules are almost exclusively absorbed on the DPPC domains.

Revision as of 14:28, 17 November 2012

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_________ ECM Proteins



FNselec.png

FNseleczoom.png





FNint.png



One of the major components of the extracellular matrix (ECM) is fibronectin, this dimeric glycoprotein is involved in numerous cell processes and has important functions in vertebrate development.

Fibronectin in the extracellular matrix interacts with the transmembrane integrins in a highly specific manner. The ECM ligand protein contains a tripeptide recognition site, Arg-Gly-Asp (RGD), responsible for the affinity of the cell surface receptors with its ligand. Atomic force microscopy images can be appreciated, these illustrations depict how fibronectin molecules are almost exclusively absorbed on the DPPC domains.