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• W2992606735 endingPage "914" @default.
• W2992606735 startingPage "898" @default.
• W2992606735 abstract "Protein kinase A has become a model system for the study of kinases, and therefore, a comprehensive understanding of the underlying molecular mechanisms in its catalytic cycle is of crucial importance. One of the aspects that has received recent attention is the role that metal cofactors play in the catalytic cycle. Although Mg2+ is the well-known physiological ion used by protein kinases, Ca2+ ions can also assist the phosphoryl transfer reaction but with lower catalytic activities. This inhibitory effect has been attributed to the ability of Ca2+ to trap the reaction products at the active site, and it has been proposed as a possible regulatory mechanism of the enzyme. Thus, in order to get a clearer understanding of these molecular events, computational simulations in the product state of PKA, in the presence of Mg2+ and Ca2+ ions, were performed through molecular dynamics (MD). Different protonation states of the active site were considered in order to model the different mechanistic pathways that have been proposed. Our results show that different protonation states of the phosphorylated serine residue at the peptide substrate (pSer21), as well as the protonation state of residue Asp166, can have a marked influence on the flexibility of regions surrounding the active site. This is the case of the glycine-rich loop, a structural motif that is directly involved in the release of the products from the PKA active site. MD simulations were capable to reproduce the crystallographic conformations but also showed other conformations not previously reported in the crystal structures that may be involved in enhancing the affinity of pSP20 to PKA in the presence of Ca2+. Hydrogen bonding interactions at the PKA-pSP20 interface were influenced whether by the protonation state of the active site or by the metal cofactor used by the enzyme. Altogether, our results provide molecular aspects into the inhibitory mechanism of Ca2+ in PKA and suggest which is the most probable protonation state of the phosphorylated product at the active site." @default.
• W2992606735 created "2019-12-13" @default.
• W2992606735 creator A5032934627 @default.
• W2992606735 creator A5047437118 @default.
• W2992606735 creator A5085462676 @default.
• W2992606735 date "2019-12-05" @default.
• W2992606735 modified "2023-10-13" @default.
• W2992606735 title "Molecular Insights into the Trapping Effect of Ca2+ in Protein Kinase A: A Molecular Dynamics Study" @default.
• W2992606735 cites W1563799197 @default.
• W2992606735 cites W1656231611 @default.
• W2992606735 cites W1691796058 @default.
• W2992606735 cites W1954353020 @default.
• W2992606735 cites W1964610218 @default.
• W2992606735 cites W1969836007 @default.
• W2992606735 cites W1970103851 @default.
• W2992606735 cites W1973437349 @default.
• W2992606735 cites W1976072883 @default.
• W2992606735 cites W1988848089 @default.
• W2992606735 cites W1991667171 @default.
• W2992606735 cites W1992014003 @default.
• W2992606735 cites W1992325160 @default.
• W2992606735 cites W1993571705 @default.
• W2992606735 cites W1994794059 @default.
• W2992606735 cites W1995042830 @default.
• W2992606735 cites W2009356149 @default.
• W2992606735 cites W2010708479 @default.
• W2992606735 cites W2014862332 @default.
• W2992606735 cites W2015505792 @default.
• W2992606735 cites W2020257412 @default.
• W2992606735 cites W2020274946 @default.
• W2992606735 cites W2031168104 @default.
• W2992606735 cites W2032804864 @default.
• W2992606735 cites W2033630329 @default.
• W2992606735 cites W2036915355 @default.
• W2992606735 cites W2037572737 @default.
• W2992606735 cites W2043224156 @default.
• W2992606735 cites W2044699597 @default.
• W2992606735 cites W2050103345 @default.
• W2992606735 cites W2052498582 @default.
• W2992606735 cites W2059412686 @default.
• W2992606735 cites W2063190248 @default.
• W2992606735 cites W2067174909 @default.
• W2992606735 cites W2077873773 @default.
• W2992606735 cites W2083392385 @default.
• W2992606735 cites W2085709611 @default.
• W2992606735 cites W2090763498 @default.
• W2992606735 cites W2094449238 @default.
• W2992606735 cites W2099144566 @default.
• W2992606735 cites W2106140689 @default.
• W2992606735 cites W2110894271 @default.
• W2992606735 cites W2116931858 @default.
• W2992606735 cites W2118233996 @default.
• W2992606735 cites W2118781403 @default.
• W2992606735 cites W2120686999 @default.
• W2992606735 cites W2122516643 @default.
• W2992606735 cites W2125074129 @default.
• W2992606735 cites W2127115175 @default.
• W2992606735 cites W2130479394 @default.
• W2992606735 cites W2130800037 @default.
• W2992606735 cites W2133625235 @default.
• W2992606735 cites W2134136251 @default.
• W2992606735 cites W2134362683 @default.
• W2992606735 cites W2139362357 @default.
• W2992606735 cites W2144288821 @default.
• W2992606735 cites W2148411491 @default.
• W2992606735 cites W2152155828 @default.
• W2992606735 cites W2152997175 @default.
• W2992606735 cites W2153076879 @default.
• W2992606735 cites W2154535504 @default.
• W2992606735 cites W2157531111 @default.
• W2992606735 cites W2159765576 @default.
• W2992606735 cites W2160262717 @default.
• W2992606735 cites W2161999370 @default.
• W2992606735 cites W2165154259 @default.
• W2992606735 cites W2166160714 @default.
• W2992606735 cites W2172864313 @default.
• W2992606735 cites W2314395966 @default.
• W2992606735 cites W2317892385 @default.
• W2992606735 cites W2342717659 @default.
• W2992606735 cites W2510044215 @default.
• W2992606735 cites W2518309182 @default.
• W2992606735 cites W2531704692 @default.
• W2992606735 cites W2601427898 @default.
• W2992606735 cites W2743259091 @default.
• W2992606735 cites W2764246110 @default.
• W2992606735 cites W2911850304 @default.
• W2992606735 cites W2924353062 @default.
• W2992606735 cites W2940323190 @default.
• W2992606735 cites W2950135346 @default.
• W2992606735 cites W2953375613 @default.
• W2992606735 cites W2972109495 @default.
• W2992606735 cites W4211145651 @default.
• W2992606735 cites W965786257 @default.
• W2992606735 doi "https://doi.org/10.1021/acs.jcim.9b00857" @default.
• W2992606735 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31804819" @default.
• W2992606735 hasPublicationYear "2019" @default.
• W2992606735 type Work @default.
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