6fak

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Human afamin orthorhombic crystal form by controlled hydrationHuman afamin orthorhombic crystal form by controlled hydration

Structural highlights

6fak is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:, , , , , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AFAM_HUMAN Vitamin E binding protein. May transport vitamin E in body fluids under conditions where the lipoprotein system is not sufficient. May be involved in the regulation and transport of vitamin E at the blood-brain barrier.[1] [2] [3]

See Also

References

  1. Voegele AF, Jerkovic L, Wellenzohn B, Eller P, Kronenberg F, Liedl KR, Dieplinger H. Characterization of the vitamin E-binding properties of human plasma afamin. Biochemistry. 2002 Dec 10;41(49):14532-8. PMID:12463752
  2. Jerkovic L, Voegele AF, Chwatal S, Kronenberg F, Radcliffe CM, Wormald MR, Lobentanz EM, Ezeh B, Eller P, Dejori N, Dieplinger B, Lottspeich F, Sattler W, Uhr M, Mechtler K, Dwek RA, Rudd PM, Baier G, Dieplinger H. Afamin is a novel human vitamin E-binding glycoprotein characterization and in vitro expression. J Proteome Res. 2005 May-Jun;4(3):889-99. doi: 10.1021/pr0500105. PMID:15952736 doi:http://dx.doi.org/10.1021/pr0500105
  3. Kratzer I, Bernhart E, Wintersperger A, Hammer A, Waltl S, Malle E, Sperk G, Wietzorrek G, Dieplinger H, Sattler W. Afamin is synthesized by cerebrovascular endothelial cells and mediates alpha-tocopherol transport across an in vitro model of the blood-brain barrier. J Neurochem. 2009 Feb;108(3):707-18. doi: 10.1111/j.1471-4159.2008.05796.x. Epub , 2008 Nov 27. PMID:19046407 doi:http://dx.doi.org/10.1111/j.1471-4159.2008.05796.x

6fak, resolution 1.90Å

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