3fgs
Crystal structure of G65R/K206E double mutant of the N-lobe human transferrinCrystal structure of G65R/K206E double mutant of the N-lobe human transferrin
Template:ABSTRACT PUBMED 19219998
DiseaseDisease
[TRFE_HUMAN] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:209300]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.[1][2]
FunctionFunction
[TRFE_HUMAN] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
About this StructureAbout this Structure
3fgs is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Mason AB, Halbrooks PJ, James NG, Byrne SL, Grady JK, Chasteen ND, Bobst CE, Kaltashov IA, Smith VC, Macgillivray RT, Everse SJ. Structural and Functional Consequences of the Substitution of Glycine 65 with Arginine in the N-Lobe of Human Transferrin (dagger). Biochemistry. 2009 Feb 16. PMID:19219998 doi:10.1021/bi802254x
- ↑ Beutler E, Gelbart T, Lee P, Trevino R, Fernandez MA, Fairbanks VF. Molecular characterization of a case of atransferrinemia. Blood. 2000 Dec 15;96(13):4071-4. PMID:11110675
- ↑ Knisely AS, Gelbart T, Beutler E. Molecular characterization of a third case of human atransferrinemia. Blood. 2004 Oct 15;104(8):2607. PMID:15466165 doi:10.1182/blood-2004-05-1751