ELIZA

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536761 occurrences (No.22 in the rank) during 5 years in the PubMed. [no cache] 500 found

329) Comparison between protein structures and multiple sequence alignment allow the identification of differences in amino acid composition in crucial regions of the enzyme, such as next to the conserved D151 and the 150-loop.

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PMID:24279589 DOI:10.1080/07391102.2013.855142

2015 Journal of biomolecular structure & dynamics

* Interface dynamics explain assembly dependency of influenza neuraminidase catalytic activity.

- Influenza virus neuraminidase (iNA) is a homotetrameric surface protein of the influenza virus and an established target for antiviral drugs. In contrast to neuraminidases (NAs) of other biological systems (non-iNAs), enzymatic activity of iNA is only observed in a quaternary assembly and iNA needs the tetramerization to mediate enzymatic activity. Obviously, differences on a molecular level between iNA and non-iNAs are responsible for this intriguing observation. Comparison between protein structures and multiple sequence alignment allow the identification of differences in amino acid composition in crucial regions of the enzyme, such as next to the conserved D151 and the 150-loop. These differences in amino acid sequence and protein tetramerization are likely to alter the dynamics of the system. Therefore, we performed molecular dynamics simulations to investigate differences in the molecular flexibility of monomers, dimers, and tetramers of iNAs of subtype N1 (avian 2004, pandemic 1918 and pandemic 2009 iNA) and as comparison the non-iNA monomer from Clostridium perfringens. We show that conformational transitions of iNA are crucially influenced by its assembly state. The protein-protein interface induces a complex hydrogen-bonding network between the 110-helix and the 150-loop, which consequently stabilizes the structural arrangement of the binding site. Therefore, we claim that these altered dynamics are responsible for the dependence of iNA's catalytic activity on the tetrameric assembly. Only the tetramerization-induced balance between stabilization and altered local flexibility in the binding site provides the appropriate arrangement of key residues for iNA's catalytic activity.

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[frequency of next (right) word to protein]

(1)76 genes,	(11)8 was	(21)3 has	(31)2 for
(2)45 genes	(12)7 level	(22)3 is	(32)2 initiation
(3)24 and	(13)6 carbonyl	(23)3 of	(33)2 level,
(4)23 levels	(14)6 coding	(24)3 oxidation,	(34)2 production
(5)18 expression	(15)5 C	(25)3 stability	(35)2 sequences
(6)12 null	(16)5 gene	(26)3 thiol	(36)2 solutions
(7)12 kinase	(17)5 isolate	(27)2 acid	(37)2 structures
(8)9 1	(18)5 kinases	(28)2 content	(38)2 that
(9)9 in	(19)4 levels,	(29)2 contents
(10)8 2	(20)3 expression,	(30)2 families

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--- WordNet output for protein --- =>タンパク質, 蛋白質, たん白質 Overview of noun protein The noun protein has 1 sense (first 1 from tagged texts) 1. (23) protein -- (any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein") --- WordNet end ---