1h44
R210L N-TERMINAL LOBE HUMAN LACTOFERRIN
|
OverviewOverview
The mammalian iron-binding proteins lactoferrin (Lf) and transferrin (Tf), bind iron very tightly, but reversibly. Despite homologous structures and, essentially identical iron binding sites, Tf begins to release iron at pH, 6.0, whereas Lf retains iron to pH approximately 3.5. This difference in, iron retention gives the two proteins different biological roles. Two, lysine residues, Lys 206 and Lys 296, which form a hydrogen-bonded, dilysine pair in human Tf, have been shown to strongly influence iron, release from the N-lobe. The equivalent residues in human Lf are Arg 210, and Lys 301, and we have here mutated Arg 210 in the N-lobe half-molecule, of human lactoferrin, Lf(N), to probe its role in iron release. The Lf(N), mutants R210G, R210E, and R210L were expressed, purified, and, ... [(full description)]
About this StructureAbout this Structure
1H44 is a [Single protein] structure of sequence from [Homo sapiens] with FE and CO3 as [ligands]. Full crystallographic information is available from [OCA].
ReferenceReference
"Dilysine trigger" in transferrins probed by mutagenesis of lactoferrin: crystal structures of the R210G, R210E, and R210L mutants of human lactoferrin., Peterson NA, Arcus VL, Anderson BF, Tweedie JW, Jameson GB, Baker EN, Biochemistry. 2002 Dec 3;41(48):14167-75. PMID:12450380
Page seeded by OCA on Mon Oct 29 19:38:15 2007