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Lactoferrin
From Proteopedia
(Difference between revisions)
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| - | <StructureSection load='1bka' size='350' side='right' caption='Human | + | <StructureSection load='1bka' size='350' side='right' caption='Human lactoferrin complex with oxalate and Fe+3 ion (PDB entry [[1bka]])' scene=''> |
== Function == | == Function == | ||
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== Relevance == | == Relevance == | ||
LTF is inhibited by nonsteroidal anti-inflammatory drugs (NSAID) like aspirin. It is a component of the immune system and has antimicrobial activity<ref>PMID:14568385</ref>. | LTF is inhibited by nonsteroidal anti-inflammatory drugs (NSAID) like aspirin. It is a component of the immune system and has antimicrobial activity<ref>PMID:14568385</ref>. | ||
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| + | == Structural highlights == | ||
| + | LTF is a bilobal protein with the N-terminal half and the C-terminal half called N-lobe and C-lobe. LTF binds with high affinity Fe+3 ion and an anion in both its N-lobe and its C-lobe<ref>PMID:8703903</ref>. The binding site is between the 2 domains of each lobe. The anion binds the Fe+3 in a 1,2 bidendate fashion. | ||
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</StructureSection> | </StructureSection> | ||
== 3D Structures of lactoferrin == | == 3D Structures of lactoferrin == | ||
Revision as of 08:39, 10 April 2016
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3D Structures of lactoferrin
Updated on 10-April-2016
References
- ↑ Actor JK, Hwang SA, Kruzel ML. Lactoferrin as a natural immune modulator. Curr Pharm Des. 2009;15(17):1956-73. PMID:19519436
- ↑ Farnaud S, Evans RW. Lactoferrin--a multifunctional protein with antimicrobial properties. Mol Immunol. 2003 Nov;40(7):395-405. PMID:14568385
- ↑ Baker HM, Anderson BF, Brodie AM, Shongwe MS, Smith CA, Baker EN. Anion binding by transferrins: importance of second-shell effects revealed by the crystal structure of oxalate-substituted diferric lactoferrin. Biochemistry. 1996 Jul 16;35(28):9007-13. PMID:8703903 doi:10.1021/bi960288y
