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Crystal structures of two mutants (K206Q, H207E) of the N‐lobe of human transferrin with increased affinity for iron
Author(s) -
Yang Amy H.W.,
Macgillivray Ross T.A.,
Chen Jie,
Luo Yaoguang,
Wang Yili,
Brayer Gary D.,
Mason Anne B.,
Woodworth Robert C.,
Murphy Michael E.P.
Publication year - 2000
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.9.1.49
Subject(s) - transferrin , mutant , chemistry , crystallography , crystal structure , stereochemistry , biochemistry , gene
The X‐ray crystallographic structures of two mutants (K206Q and H207E) of the N‐lobe of human transferrin (hTF/2N) have been determined to high resolution (1.8 and 2.0 Å, respectively). Both mutant proteins bind iron with greater affinity than native hTF/2N. The structures of the K206Q and H207E mutants show interactions (both H‐bonding and electrostatic) that stabilize the interaction of Lys296 in the closed conformation, thereby stabilizing the iron bound forms.