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structural comparison of human serum transferrin and human lactoferrin

Wally, Jeremy ; Buchanan, Susan K

Biometals, 2007-06, Vol.20 (3-4), p.249-262 [Periódico revisado por pares]

Netherlands: New York : Kluwer Academic Publishers-Plenum Publishers

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Título:
structural comparison of human serum transferrin and human lactoferrin
Autor: Wally, Jeremy ; Buchanan, Susan K
Assuntos: Amino Acid Sequence ; Animals ; Antibiotics ; Antiinfectives and antibacterials ; Bacteria ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bacterial transferrin receptor ; Blood ; Body fluids ; Crystal structure ; Disulfides - chemistry ; Fluids ; Human ; Human transferrin receptor ; Humans ; Iron ; Iron - metabolism ; Iron transport ; Lactoferrin ; Lactoferrin - chemistry ; Lactoferrin - genetics ; Lactoferrin - metabolism ; Membrane proteins ; Models, Molecular ; Molecular Sequence Data ; Outer membrane proteins ; Pathogenic bacteria ; Protein Structure, Quaternary ; Protein transport ; Proteins ; Receptors ; Receptors, Cell Surface - metabolism ; Receptors, Transferrin - metabolism ; Secretions ; Sequence Alignment ; Serum ; Serums ; Transferrin ; Transferrin - chemistry ; Transferrin - genetics ; Transferrin - metabolism ; Transferrins ; Transportation systems
É parte de: Biometals, 2007-06, Vol.20 (3-4), p.249-262
Notas: http://dx.doi.org/10.1007/s10534-006-9062-7
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Descrição: The transferrins are a family of proteins that bind free iron in the blood and bodily fluids. Serum transferrins function to deliver iron to cells via a receptor-mediated endocytotic process as well as to remove toxic free iron from the blood and to provide an anti-bacterial, low-iron environment. Lactoferrins (found in bodily secretions such as milk) are only known to have an anti-bacterial function, via their ability to tightly bind free iron even at low pH, and have no known transport function. Though these proteins keep the level of free iron low, pathogenic bacteria are able to thrive by obtaining iron from their host via expression of outer membrane proteins that can bind to and remove iron from host proteins, including both serum transferrin and lactoferrin. Furthermore, even though human serum transferrin and lactoferrin are quite similar in sequence and structure, and coordinate iron in the same manner, they differ in their affinities for iron as well as their receptor binding properties: the human transferrin receptor only binds serum transferrin, and two distinct bacterial transport systems are used to capture iron from serum transferrin and lactoferrin. Comparison of the recently solved crystal structure of iron-free human serum transferrin to that of human lactoferrin provides insight into these differences.
Editor: Netherlands: New York : Kluwer Academic Publishers-Plenum Publishers
Idioma: Inglês;Holandês

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structural comparison of human serum transferrin and human lactoferrin

Wally, Jeremy ; Buchanan, Susan K

Netherlands: New York : Kluwer Academic Publishers-Plenum Publishers

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