Impact of pathological mutations on Alpha-Sarcoglycan Protein Structure

Table 1.1 Types of MDs and their Symptoms
Figure 1: Alpha-Sarcoglycan structure predicted using homology modeling. (A) SGCA protein prominently depicts anti parallel beta sheets and extended loops. (B) Replacing aspartic acid to glycine residue at the position 97 showed no effect on the overall structure of the protein.
Figure 2: Comparison between SGCA WT and D97G mutant protein intramolecular molecular interactions. D97G point mutation results in the loss of multiple side chain interactions with the neighboring amino acids.
Figure 3: Alpha-Sarcoglycan structure predicted using homology modeling. (A) SGCA protein prominently depicts anti parallel beta sheets and extended loops. (B) Replacing leucine to proline residue at the position 31 showed no effect on the overall structure of the protein.
Figure 4: Comparison between SGCA WT and L31P mutant protein intramolecular molecular interactions. L31P point mutation results in the loss of multiple side chain interactions with the neighboring amino acids and a formation of a ring structure as opposed to the original branch-like structure.
Figure 5: Alpha-Sarcoglycan structure predicted using homology modeling. (A) SGCA protein prominently depicts anti parallel beta sheets and extended loops. (B) Replacing cysteine to arginine residue at the position 77 showed no effect on the overall structure of the protein.
Figure 6: Comparison between SGCA WT and R77C mutant protein intramolecular molecular interactions. R77C point mutation results in the loss of multiple side chain interactions with the neighboring amino acids.
Figure 7: Alpha-Sarcoglycan structure predicted using homology modeling. (A) SGCA protein prominently depicts anti parallel beta sheets and extended loops. (B) Replacing arginine to proline residue at the position 73 resulted in shortening of one beta sheet strand.
Figure 8: Comparison between SGCA WT and P73R mutant protein intramolecular molecular interactions. P73R point mutation results in the loss of multiple side chain interactions with the neighboring amino acids and a change from a ring structure to a branch-like structure.
Figure 9: Alpha-Sarcoglycan structure predicted using homology modeling. (A) SGCA protein prominently depicts anti parallel beta sheets and extended loops. (B) Replacing leucine to proline residue at the position 73 resulted in shortening of one beta sheet strand.
Figure 10: Comparison between SGCA WT and P73L mutant protein intramolecular molecular interactions. P73L point mutation results in the loss of multiple side chain interactions with the neighboring amino acids and a change from a ring structure to a branch-like structure.

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