Lactoferrin

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Function

Lactoferrin or lactotransferrin (LTF) is found in secretory fluids. LTF interacts with DNA, RNA, polysaccharides and heparin[1]. For detailed discussion of human lactoferrin see Human lactoferrin.

Relevance

LTF is inhibited by nonsteroidal anti-inflammatory drugs (NSAID) like aspirin. It is a component of the immune system and has antimicrobial activity[2]. LTF can be used as a marker for inflammatory bowel disease[3].

Structural highlights

LTF is a bilobal protein with the . LTF binds with high affinity Fe+3 ion and an anion in both its N-lobe and its C-lobe[4]. The binding site is between the 2 domains of each lobe.

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The .

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The .


Human lactoferrin complex with oxalate and Fe+3 ion (PDB entry 1bka)

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3D Structures of lactoferrin3D Structures of lactoferrin

Updated on 15-June-2023

ReferencesReferences

  1. Actor JK, Hwang SA, Kruzel ML. Lactoferrin as a natural immune modulator. Curr Pharm Des. 2009;15(17):1956-73. PMID:19519436
  2. Farnaud S, Evans RW. Lactoferrin--a multifunctional protein with antimicrobial properties. Mol Immunol. 2003 Nov;40(7):395-405. PMID:14568385
  3. Kayazawa M, Saitoh O, Kojima K, Nakagawa K, Tanaka S, Tabata K, Matsuse R, Uchida K, Hoshimoto M, Hirata I, Katsu K. Lactoferrin in whole gut lavage fluid as a marker for disease activity in inflammatory bowel disease: comparison with other neutrophil-derived proteins. Am J Gastroenterol. 2002 Feb;97(2):360-9. PMID:11866274 doi:http://dx.doi.org/10.1111/j.1572-0241.2002.05470.x
  4. 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

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Michal Harel, Alexander Berchansky