Structure-Based Virtual Screening of Protein Tyrosine Phosphatase Inhibitors: Significance, Challenges, and Solutions
Phosphorylation, a critical mechanism in biological systems, is estimated to be indispensable for about 30% of key biological activities, such as cell cycle progression, migration, and division. It is synergistically balanced by kinases and phosphatases, and any deviation from this balance leads to...
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Veröffentlicht in: | Journal of microbiology and biotechnology 2017-05, Vol.27 (5), p.878-895 |
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description | Phosphorylation, a critical mechanism in biological systems, is estimated to be indispensable for about 30% of key biological activities, such as cell cycle progression, migration, and division. It is synergistically balanced by kinases and phosphatases, and any deviation from this balance leads to disease conditions. Pathway or biological activity-based abnormalities in phosphorylation and the type of involved phosphatase influence the outcome, and cause diverse diseases ranging from diabetes, rheumatoid arthritis, and numerous cancers. Protein tyrosine phosphatases (PTPs) are of prime importance in the process of dephosphorylation and catalyze several biological functions. Abnormal PTP activities are reported to result in several human diseases. Consequently, there is an increased demand for potential PTP inhibitory small molecules. Several strategies in structure-based drug designing techniques for potential inhibitory small molecules of PTPs have been explored along with traditional drug designing methods in order to overcome the hurdles in PTP inhibitor discovery. In this review, we discuss druggable PTPs and structure-based virtual screening efforts for successful PTP inhibitor design. |
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It is synergistically balanced by kinases and phosphatases, and any deviation from this balance leads to disease conditions. Pathway or biological activity-based abnormalities in phosphorylation and the type of involved phosphatase influence the outcome, and cause diverse diseases ranging from diabetes, rheumatoid arthritis, and numerous cancers. Protein tyrosine phosphatases (PTPs) are of prime importance in the process of dephosphorylation and catalyze several biological functions. Abnormal PTP activities are reported to result in several human diseases. Consequently, there is an increased demand for potential PTP inhibitory small molecules. Several strategies in structure-based drug designing techniques for potential inhibitory small molecules of PTPs have been explored along with traditional drug designing methods in order to overcome the hurdles in PTP inhibitor discovery. 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In this review, we discuss druggable PTPs and structure-based virtual screening efforts for successful PTP inhibitor design.</description><subject>Allosteric targeting</subject><subject>cancers</subject><subject>diabetes</subject><subject>drug designing</subject><subject>molecular docking</subject><subject>protein tyrosine phosphatases</subject><issn>1017-7825</issn><issn>1738-8872</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>JDI</sourceid><recordid>eNo9kE1LAzEYhBdRsFZ_gZdcvHUhn03qrRY_qoUWtnhd3t0k3dg1KUn20H_vguJphuGZOcxFMSGSqVIpSS9Hj4kspaLiurhJ6QvjOaFqPimGKsehzUM05RMko9Gni3mAHlVtNMY7f0DBol0M2TiP9ucYkvMG7bqQTh3ksYLWvnONyyGmR1S5g3fWteBbM0OrDvre-INJMwReoyr0Q3bBp9viykKfzN2fTov9y_N-9VZutq_r1XJTHgUWJRjb6JbThnCuCNZaAmUCGMyxXTSCcUqBcUkFsdwYzSjmYMe44bZhC9qyafHwO3t0Kbva69TX78uPLR3PIAqLcZVTKUbu_p9L9Sm6b4jnmgmiFoKyH8PcYaQ</recordid><startdate>20170531</startdate><enddate>20170531</enddate><creator>Reddy, Rallabandi Harikrishna</creator><creator>Kim, Hackyoung</creator><creator>Cha, Seungbin</creator><creator>Lee, Bongsoo</creator><creator>Kim, Young Jun</creator><general>한국미생물생명공학회</general><scope>HZB</scope><scope>Q5X</scope><scope>JDI</scope></search><sort><creationdate>20170531</creationdate><title>Structure-Based Virtual Screening of Protein Tyrosine Phosphatase Inhibitors: Significance, Challenges, and Solutions</title><author>Reddy, Rallabandi Harikrishna ; Kim, Hackyoung ; Cha, Seungbin ; Lee, Bongsoo ; Kim, Young Jun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-k505-aefbdc42b144810dd7a235a3a60f9b53422a347251f4eed3204af534b4fb392c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>kor</language><creationdate>2017</creationdate><topic>Allosteric targeting</topic><topic>cancers</topic><topic>diabetes</topic><topic>drug designing</topic><topic>molecular docking</topic><topic>protein tyrosine phosphatases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Reddy, Rallabandi Harikrishna</creatorcontrib><creatorcontrib>Kim, Hackyoung</creatorcontrib><creatorcontrib>Cha, Seungbin</creatorcontrib><creatorcontrib>Lee, Bongsoo</creatorcontrib><creatorcontrib>Kim, Young Jun</creatorcontrib><collection>KISS</collection><collection>Korean Studies Information Service System (KISS) B-Type</collection><collection>KoreaScience</collection><jtitle>Journal of microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Reddy, Rallabandi Harikrishna</au><au>Kim, Hackyoung</au><au>Cha, Seungbin</au><au>Lee, Bongsoo</au><au>Kim, Young Jun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure-Based Virtual Screening of Protein Tyrosine Phosphatase Inhibitors: Significance, Challenges, and Solutions</atitle><jtitle>Journal of microbiology and biotechnology</jtitle><addtitle>Journal of Microbiology and Biotechnology</addtitle><date>2017-05-31</date><risdate>2017</risdate><volume>27</volume><issue>5</issue><spage>878</spage><epage>895</epage><pages>878-895</pages><issn>1017-7825</issn><eissn>1738-8872</eissn><abstract>Phosphorylation, a critical mechanism in biological systems, is estimated to be indispensable for about 30% of key biological activities, such as cell cycle progression, migration, and division. It is synergistically balanced by kinases and phosphatases, and any deviation from this balance leads to disease conditions. Pathway or biological activity-based abnormalities in phosphorylation and the type of involved phosphatase influence the outcome, and cause diverse diseases ranging from diabetes, rheumatoid arthritis, and numerous cancers. Protein tyrosine phosphatases (PTPs) are of prime importance in the process of dephosphorylation and catalyze several biological functions. Abnormal PTP activities are reported to result in several human diseases. Consequently, there is an increased demand for potential PTP inhibitory small molecules. Several strategies in structure-based drug designing techniques for potential inhibitory small molecules of PTPs have been explored along with traditional drug designing methods in order to overcome the hurdles in PTP inhibitor discovery. 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subjects | Allosteric targeting cancers diabetes drug designing molecular docking protein tyrosine phosphatases |
title | Structure-Based Virtual Screening of Protein Tyrosine Phosphatase Inhibitors: Significance, Challenges, and Solutions |
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