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Can I read Modeling of the structure of the Haemophilus influenzae heme-binding protein suggests a mode of heme interaction on EtoBox?
Modeling of the structure of the Haemophilus influenzae heme-binding protein suggests a mode of heme interaction by Pete Dunten; Sherry L. Mowbray is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
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## Abstract The structure and function of the periplasmic heme‐binding protein HbpA of __Haemophilus influenzae__ were investigated. This protein is involved in the import of heme into the bacteria through the inner membrane, and thus is a key element of the organism's ability to survive in blood. A high degree of sequence similarity between HbpA and the dipeptide‐binding protein of __Escherichia coli__ is suggested to be the result of a functional relationship. An HbpA model built using the dipeptide‐binding protein suggests a mode of heme binding that is distinct from those known in proteins of the human host. These results provide a starting point for rational drug design.
Who reads Modeling of the structure of the Haemophilus influenzae heme-binding protein suggests a mode of heme interaction?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Pete Dunten; Sherry L. Mowbray
- Publisher
- Cold Spring Harbor Laboratory Press; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0961-8368)
- Published
- 1995
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)