User:Nilima Kolli/sandbox 1
From Proteopedia
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A [[CBI Molecule]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | A [[CBI Molecule]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | ||
| - | Human protective protein/cathepsin A (PPCA | + | Human protective protein/cathepsin A (PPCA) is a serine carboxypeptidase that also has chaperoning function towards two other lysosomal enzymes, Neu1 and Glb1. |
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<applet load='1ivy' size='[450,338]' frame='true' align='right' | <applet load='1ivy' size='[450,338]' frame='true' align='right' | ||
caption='Human Protective Protein/Cathepsin A (PPCA, 1IVY)' scene='User:Nilima_Kolli/sandbox_1/Homodimer_ppca/1'/> | caption='Human Protective Protein/Cathepsin A (PPCA, 1IVY)' scene='User:Nilima_Kolli/sandbox_1/Homodimer_ppca/1'/> | ||
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| + | The homodimer of <scene name='User:Nilima_Kolli/sandbox_1/Homodimer_ppca/1'>PPCA</scene> is shown here in cartoon representation. The active site residues are in red with the disulphides in yellow. The catalytically competent active site is blocked by the 'blocking peptide' shown in cyan. The excision peptide shown in dark blue is positioned above the blocking peptide thus completely occluding the active site. The excision peptide is removed during processing which is assumed to result in local conformational changes that then remove the blocking peptide from occluding the active site. | ||
Revision as of 19:46, 28 April 2010
A CBI Molecule being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.
Human protective protein/cathepsin A (PPCA) is a serine carboxypeptidase that also has chaperoning function towards two other lysosomal enzymes, Neu1 and Glb1.
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The homodimer of is shown here in cartoon representation. The active site residues are in red with the disulphides in yellow. The catalytically competent active site is blocked by the 'blocking peptide' shown in cyan. The excision peptide shown in dark blue is positioned above the blocking peptide thus completely occluding the active site. The excision peptide is removed during processing which is assumed to result in local conformational changes that then remove the blocking peptide from occluding the active site.
