6jbp

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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Mortality due to snakebite is a serious public health problem and available therapeutics are known to induce debilitating side effects. Traditional medicine suggests that seeds of Mucuna pruriens can provide protection against the effects of snakebite. Our aim is to identify the protein/s that may be important for snake venom neutralization and elucidate their mechanism of action. To this end, we have identified and purified a protein from Mucuna pruriens, which we have named MP-4. The full-length polypeptide sequence of MP-4 was obtained through N-terminal sequencing of peptide fragments. Sequence analysis suggested that the protein may belong to the Kunitz-type protease inhibitor (KTPI) family and therefore may potentially neutralize the proteases present in snake venom. Using various structural and biochemical tools coupled with in vivo assays, we are able to show that MP-4 does not afford direct protection against snake venom because it is actually a poor inhibitor of serine proteases. Further experiments showed that antibodies generated against MP-4 cross-react with the whole venom and provide protection to mice against Echis carinatus snake venom. This study shows that the MP-4 contributes significantly to the snake venom neutralization activity of Mucuna pruriens seeds through an indirect antibody-mediated mechanism.
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The structure of the MP-4 protein was previously determined at a resolution of 2.8 A. Owing to the unavailability of gene-sequence information at the time, the side-chain assignment was carried out on the basis of a partial sequence available through Edman degradation, sequence homology to orthologs and electron density. The structure of MP-4 has now been determined at a higher resolution (2.22 A) in another space group and all of the structural inferences that were presented in the previous report of the structure were validated. In addition, the present data allowed an improved assignment of side chains and enabled further analysis of the MP-4 structure, and the accuracy of the assignment was confirmed by the recently available gene sequence. The study reinforces the traditional concept that conservative interpretations of relatively low-resolution structures remain correct even with the availability of high-resolution data.
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MP-4 contributes to snake venom neutralization by Mucuna pruriens seeds through an indirect antibody-mediated mechanism.,Kumar A, Gupta C, Nair DT, Salunke DM J Biol Chem. 2016 Mar 17. pii: jbc.M115.699173. PMID:26987900<ref>PMID:26987900</ref>
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The structure of MP-4 from Mucuna pruriens at 2.22 A resolution.,Jain A, Kumar A, Shikhi M, Kumar A, Nair DT, Salunke DM Acta Crystallogr F Struct Biol Commun. 2020 Feb 1;76(Pt 2):47-57. doi:, 10.1107/S2053230X20000199. Epub 2020 Feb 3. PMID:32039885<ref>PMID:32039885</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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*[[Journal:Acta Cryst F:S2053230X20000199|Journal:Acta Cryst F:S2053230X20000199]]
== References ==
== References ==
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Revision as of 10:19, 26 February 2020

Structure of MP-4 from Mucuna pruriens at 2.22 Angstroms

PDB ID 6jbp

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