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. A. Conformational signals in the C-terminal domain of methionine adenosyltransferase I/III determine its nucleocytoplasmic distribution. Abstract The methyl donor S -adenosylmethionine is synthesized ...
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–competent conformations. However, to avoid spurious signaling, such states must necessarily be highly unstable to ensure that the default folding pathway predominates in the absence of ligand.In recent ...
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: SH4, unique domain, SH3, SH2, kinase (catalytic), and the C-terminal regulatory region. The sequence homology within the family is rather high with the exception of the N-terminal region comprising ...
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riboswitch mechanisms involve regulation at the level of premature termination of transcription or translation initiation. Riboswitches that affect transcription termination undergo a conformational switch ...
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and the accumulation of sulfoxidized methionines. Computational and synthetic approaches have shown that this change in the polarity of M206 and M213 impacts the C-terminal domain native α-fold allowing the flexibility ...
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the amino-terminal site with the two in-tandem cGMP-binding pockets. The C-terminal part of the protein harbors the catalytic domain, which consists of a MgATP-binding pocket and the substrate-binding site. ...
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conformational substrates of the C-terminal domain of calmodulin (cCaM) by NMR N 15 spin relaxation experiments. A comparison of exchange rates as a function of Ca 2+ Ca 2 + concentration has established ...
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and diverse roles in plant development and signalling, and act as integrators of signals from multiple plant growth regulatory and environmental inputs. Possessing an intrinsically disordered N-terminal domain ...
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it deviates from this simple picture and also because the existence and importance of it has only recently been appreciated [ 7 ]. The amino terminal NH 2 of the initiator Methionine provides a potential ...
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the N- and C-terminal lobes of the kinase domain. Assembly of the regulatory spine has been proposed to be a crucial step in the activation of protein kinases, and this structure is disrupted ...
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