Asp ligand provides the trigger for closure of transferrin molecules. Direct evidence from X-ray scattering studies of site-specific mutants of the N-terminal half-molecule of human transferrin

Autor:	J G, Grossmann, A B, Mason, R C, Woodworth, M, Neu, P F, Lindley, S S, Hasnain
Rok vydání:	1993
Předmět:	Models Molecular Aspartic Acid Iron X-Rays Mutagenesis Site-Directed Transferrin Humans Scattering Radiation Hydrogen Bonding Ligands
Zdroj:	Journal of molecular biology. 231(3)
ISSN:	0022-2836
Popis:	Recent X-ray crystallographic and solution X-ray scattering studies have shown that transferrins (serum transferrin, lactoferrin and ovotransferrin) undergo a major conformational change when iron is incorporated into the molecule. Apo-proteins show a structure with open interdomain clefts which close when iron is bound. The closed conformation has been suggested as an important step in the receptor recognition. Here, we report X-ray solution scattering experiments of the mutated N-terminal fragment of human serum transferrin with Asp63--Ser (Cys). The data provide the first direct experimental evidence for the existence of a trigger mechanism for the closure of the interdomain cleft and that this trigger mechanism is disrupted by mutation of Asp63, the only ligand of iron from domain I.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::d50bd98a55be98b80ae39520621094ab https://pubmed.ncbi.nlm.nih.gov/8515439 Zobrazit plný text záznamu