Structure and Phylogeny of Pentraxins

Structure and Phylogeny of Pentraxins

Registration ID: IJNRD_223791

Published ID: IJNRD2406300

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Dibyajyoti Dwari

The human plasma proteins c-reactive protein (CRP) and serum amyloid P component (SAP) are one of the considerable current interest as targets for drug interventions to target inflammatory and amyloid deposition diseases respectively. They are homologous members of a wider protein family, the pentraxin family, that share the same jelly-roll topology of subunit architecture and in many cases, a pentameric arrangement of subunits in their quaternary structure. Despite their similarity and likely evolution from a gene duplication event, the human proteins display distinct specificity for calcium-dependent binding of ligands that likely underlies their role in biology. There is also considerable current speculation that different oligomeric states of c-reactive protein may exhibit different functionalities. The evolutionary history of the protein family is extended with related proteins present in most vertebrates and some invertebrates. The protein fold is also displayed in some plant proteins like concanavalin A and as a domain in bacterial toxins like botulinum toxin. The growing database of amino acid sequences arising from gene sequencing provides the results of an extensive mutagenesis experiment of nature, where the pentraxins have adapted to different physiological contexts. A study of the properties of these molecules may provide insights into the behavior of human proteins. For example, it is known that the female hamster pentraxin recognizes phosphocholine and amyloid fibers, specific ligands for the different human proteins. The zebrafish protein assembles as trimers while the protein from the horse-shoe crab forms heptamers. With regards to that human pentraxins are pentameric. Therefore studies regarding these proteins can give a fundamental understanding about the structure and function of these proteins. The structural variation is also found in case different type of species in the evolution due various biological factors. Can these molecules inform us about the hypothesized instability of human CRP? The main objective of this study is to find out more information about the structure and behavior of this proteins.

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"Structure and Phylogeny of Pentraxins ", IJNRD - INTERNATIONAL JOURNAL OF NOVEL RESEARCH AND DEVELOPMENT (www.IJNRD.org), ISSN:2456-4184, Vol.9, Issue 6, page no.d115-d133, June-2024, Available :https://ijnrd.org/papers/IJNRD2406300.pdf

Volume 9 Issue 6, June-2024

Pages : d115-d133

Paper Reg. ID: IJNRD_223791

Published Paper Id: IJNRD2406300

Downloads: 000121134

Research Area: Life Sciences 

Country: Balasore, Odisha, India

Published Paper PDF: https://ijnrd.org/papers/IJNRD2406300.pdf

Published Paper URL: https://ijnrd.org/viewpaperforall?paper=IJNRD2406300

Journal Name: INTERNATIONAL JOURNAL OF NOVEL RESEARCH AND DEVELOPMENT(IJNRD)

ISSN: 2456-4184 | IMPACT FACTOR: 8.76 Calculated By Google Scholar | ESTD YEAR: 2016

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