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475194 occurrences (No.33 in the rank) during 5 years in the PubMed. [no cache] 500 found

326) Therefore, we claim that these altered dynamics are responsible for the dependence of iNA's catalytic activity on the tetrameric assembly.

--- ABSTRACT ---

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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(1)70 of	(13)6 patterns	(25)3 but	(37)2 functional
(2)54 null	(14)5 may	(26)3 changes	(38)2 increased
(3)49 and	(15)5 using	(27)3 for	(39)2 induces
(4)45 in	(16)5 with	(28)3 measured	(40)2 level
(5)17 was	(17)4 at	(29)3 through	(41)2 or
(6)11 against	(18)4 levels	(30)2 Questionnaire	(42)2 over
(7)10 during	(19)4 on	(31)2 after	(43)2 promotion
(8)9 (PA)	(20)4 which	(32)2 between	(44)2 resumption
(9)8 is	(21)4 while	(33)2 calcium	(45)2 than
(10)7 to	(22)3 among	(34)2 compared	(46)2 that
(11)7 were	(23)3 are	(35)2 decreased	(47)2 via
(12)6 by	(24)3 as	(36)2 diary	(48)2 when

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--- WordNet output for activity --- =>活動, 活躍, 働き, 動き, 活気 Overview of noun activity The noun activity has 6 senses (first 3 from tagged texts) 1. (43) activity -- (any specific behavior; "they avoided all recreational activity") 2. (36) action, activity, activeness -- (the state of being active; "his sphere of activity"; "he is out of action") 3. (13) bodily process, body process, bodily function, activity -- (an organic process that takes place in the body; "respiratory activity") 4. activity -- ((chemistry) the capacity of a substance to take part in a chemical reaction; "catalytic activity") 5. natural process, natural action, action, activity -- (a process existing in or produced by nature (rather than by the intent of human beings); "the action of natural forces"; "volcanic activity") 6. activeness, activity -- (the trait of being active; moving or acting rapidly and energetically; "the level of activity declines with age") --- WordNet end ---