Mutant MAD7 Protein K169 D529 Substitutions
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Solution Overview
Problem
Current MAD7 proteins used in genome editing have limited target-site cleavage activity, which hampers the efficiency of genetic modifications in organisms.
Innovation Solution
A mutant MAD7 protein with specific amino acid sequence modifications, including substitutions at positions K169 and D529, and optionally Y1086, K970, and E1227, is developed to enhance target-site cleavage activity.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If wild-type MAD7 protein is used, then the protein structure is stable and well-characterized, but the target-site cleavage activity is insufficient
Solution Approach 1:
The patent applies parameter changes by introducing specific amino acid substitutions at positions K169 and D529 in the MAD7 protein sequence. These parameter changes in the protein's molecular structure result in enhanced target-site cleavage activity while maintaining protein stability and functionality.
2Reliability
If mutations are introduced to improve cleavage activity, then target-site cleavage activity increases, but protein stability may be compromised
Solution Approach 1:
The patent applies local quality by making targeted amino acid substitutions at specific positions (K169 and D529) rather than widespread mutations. This localized modification approach allows improvement of cleavage activity in specific functional regions while preserving the overall structural stability and fold of the MAD7 protein.
Data Source
AI summary
A mutant MAD7 protein with higher target-site cleavage activity is provided. The mutant MAD7 protein includes an amino acid sequence B obtained by introducing mutations into an amino acid sequence A represented by SEQ ID NO:1, the amino acid sequence B including amino-acid substitution mutations of K169 and D529 in the amino acid sequence A.