Sandbox GGC9: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
The collagen complex with binding protein represent in this <scene name='75/752271/Collagenadhesincomplex/2'>view</scene>. Furthermore, this <scene name='75/752271/Procollagen/1'>Ttriple helices</scene> represents the structure of procollagen (triple α-chain). The structural of hydroxyproline redisue of <scene name='75/752271/Hypresidue/2'> | The collagen complex with binding protein represent in this <scene name='75/752271/Collagenadhesincomplex/2'>view</scene>. Furthermore, this <scene name='75/752271/Procollagen/1'>Ttriple helices</scene> represents the structure of procollagen (triple α-chain). The structural of hydroxyproline redisue of <scene name='75/752271/Hypresidue/2'>Hydroxylproline</scene>. | ||
Refer back to the the collagen-binding site of human Type I and Type III collagen, VWF-A3 is distinctly different from that of the homologous integrin α2 I domain, which has a hydrophilic binding site located at the top face of the domain. Based on the surface characteristics of the collagen-binding site, the proposal is that collagen-binding protein interact with collagen sequences containing positively charged and hydrophobic residues. The <scene name='75/752271/Procollagenii/1'>particular amino acid residues</scene>s in the binding protein in this case CNA interact with the residue of the collagen base on the polarity and non-polar molecules. Therefore, bacterial adhesion follows the same rule as eukaryotic binding factors. | Refer back to the the collagen-binding site of human Type I and Type III collagen, VWF-A3 is distinctly different from that of the homologous integrin α2 I domain, which has a hydrophilic binding site located at the top face of the domain. Based on the surface characteristics of the collagen-binding site, the proposal is that collagen-binding protein interact with collagen sequences containing positively charged and hydrophobic residues. The <scene name='75/752271/Procollagenii/1'>particular amino acid residues</scene>s in the binding protein in this case CNA interact with the residue of the collagen base on the polarity and non-polar molecules. Therefore, bacterial adhesion follows the same rule as eukaryotic binding factors. | ||
