Substrate uptake and protein stability relationship in mammalian histidine decarboxylase

There is some evidence linking the substrate entrance in the active site of mammalian histidine decarboxylase and an increased stability against proteolytic degradation. In this work, we study the basis of this relationship by means of protein structure network analysis and molecular dynamics simula...

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Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2010-01, Vol.78 (1), p.154-161
Hauptverfasser:	Pino-Ángeles, A., Morreale, A., Negri, A., Sánchez-Jiménez, F., Moya-García, A. A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals essential dynamics histidine decarboxylase Histidine Decarboxylase - chemistry Histidine Decarboxylase - metabolism Mammals - metabolism Molecular Dynamics Simulation Motion Protein Binding Protein Conformation Protein Multimerization Protein Stability protein structure network stability Substrate Specificity
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