The pursuit of a novel structural motif that can shed light on the key functional attributes is a primary focus in the study of protein folding disorders. Decades of research on Alzheimer's disease (AD) have centered on the Amyloid β (Aβ) pathway, highlighting its significance in understanding the disorder. The diversity in the Aβ pathway and the possible silent tracks which are yet to discover, makes it exceedingly intimidating to the interdisciplinary scientific community. Over the course of AD research, Aβ has consistently been at the forefront of scientific inquiry and discussion. In this review, we epitomize the role of a potential structural motif (GxxxG motif) that may provide a new horizon to the Aβ conflict. We emphasize on how comprehensive understanding of this motif from a structure-function perspective may pave the way for designing novel therapeutics intervention in AD and related diseases.
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| http://dx.doi.org/10.1021/acsbiomedchemau.3c00055 | DOI Listing |
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Article Synopsis
- * In a study of 6000 obligate homodimeric complexes, AXXXA was found in 27,000 occurrences, while GXXXG appeared 18,000 times, mainly in obligate dimers compared to transient and heterodimers.
- * AXXXA motifs play a key role in stabilizing the structure of proteins through specific hydrophobic interactions; replacing terminal Ala residues with Gly significantly reduces motif occurrences, suggesting its importance for protein design and therapeutic development.
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