THE HELIX-TURN-HELIX AS A SCAFFOLD FOR CHIMERIC NUCLEASE DESIGN

Autor:	Sonya J. Franklin, Joel T. Welch
Rok vydání:	2005
Předmět:	chemistry.chemical_classification Scaffold biology Calmodulin Chemistry Stereochemistry Protein design Active site Helix-turn-helix Peptide engrailed Inorganic Chemistry Crystallography biology.protein Chimeric nuclease
Zdroj:	Comments on Inorganic Chemistry. 26:127-164
ISSN:	1548-9574 0260-3594
Popis:	De novo design is a powerful tool to investigate the active site of enzymatic metalloproteins, in a smaller, defined model system. It is also a way to build or combine activity and selectivity in unique ways, not seen biologically. We are utilizing protein design to build artificial endonucleases, and to investigate fundamental questions of metallonuclease structure and function. We have focused on designing peptide constructs comprising geometrically similar turns from unrelated proteins, in particular the Ca-binding EF-hand motif of calmodulin and the helix-turn-helix motif (HTH) of engrailed homeodomain. By substituting the calcium-binding (and thus lanthanide-binding) loop in place of the “turn” of engrailed HTH, hydrolytically active, DNA-binding constructs were created. The NMR solution structure of one La-binding chimera (P3W), calculated based on NOE volume integrals, demonstrated that the 33-mer peptide retains the parental helix-turn-helix structure when bound to lanthanide ions. The bi...
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::5462c29d5c6083875e400b24758b2a03 https://doi.org/10.1080/02603590500201188 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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