Factor IX: Difference between revisions
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'''Mutations:''' | '''Mutations:''' | ||
Phe496 correspond to residue 16: Consensus phenylalanine to alanine leads to a reduced affinity of the internal propeptide for the propeptide binding site. | Phe496 correspond to residue 16: Consensus phenylalanine to alanine leads to a reduced affinity of the internal propeptide for the propeptide binding site. | ||
Val502 corresponds to position 10, Consensus val to alanine, leads to an increase in the affinity of the proposed internal propeptide for the propeptide binding site. | Val502 corresponds to position 10, Consensus val to alanine, leads to an increase in the affinity of the proposed internal propeptide for the propeptide binding site. | ||
Glutamine 503 corresponds to position 9, Consensus Gln to Arg leads to a reduced affinity of the internal propeptide for the propeptide binding site. Consensus Gln to Asn, leads the consensus residue to have a modest increase in the apparent affinity. | Glutamine 503 corresponds to position 9, Consensus Gln to Arg leads to a reduced affinity of the internal propeptide for the propeptide binding site. Consensus Gln to Asn, leads the consensus residue to have a modest increase in the apparent affinity. | ||
Pro 504 corresponds to position 8, not a highly conserved position; however, the propeptide may have an -helical structure (6), and in this case the proline will disrupt the substrate propeptide helix. Changing proline 504 to the consensus sequence residue, glutamine, has a small increase in the affinity of the internal propeptide for its binding site. | Pro 504 corresponds to position 8, not a highly conserved position; however, the propeptide may have an -helical structure (6), and in this case the proline will disrupt the substrate propeptide helix. Changing proline 504 to the consensus sequence residue, glutamine, has a small increase in the affinity of the internal propeptide for its binding site. | ||
These mutations identified that residues 495-513 in the carboxylase act as an internal propeptide binding site (7). | These mutations identified that residues 495-513 in the carboxylase act as an internal propeptide binding site (7). | ||
