1dtg

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models PDB ID 1dtg Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1dtg, resolution 2.40Å ()
Ligands:	,
Structural annotation: Resources: CATH : 1Dtga01, 1Dtga02 InterPro : Ipr001156 Pfam : PF00405 SCOP : d1dtga_ UniProt : P02787
Functional annotation: Cellular component: endocytic vesicle endosome extracellular region Biological process: transport cellular iron ion homeostasis iron ion transport ion transport Molecular function: iron ion binding ferric iron binding metal ion binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Contents 1 HUMAN TRANSFERRIN N-LOBE MUTANT H249E 2 Disease 3 Function 4 About this Structure 5 See Also 6 Reference

HUMAN TRANSFERRIN N-LOBE MUTANT H249E

Template:ABSTRACT PUBMED 10684598

Disease

[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]

Function

[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 Structure

1dtg is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

• Cartoon backbone representation
• Secondary structure
• Sheets in Proteins
• Spacefilling representation
• Transferrin

Reference

• MacGillivray RT, Bewley MC, Smith CA, He QY, Mason AB, Woodworth RC, Baker EN. Mutation of the iron ligand His 249 to Glu in the N-lobe of human transferrin abolishes the dilysine "trigger" but does not significantly affect iron release. Biochemistry. 2000 Feb 15;39(6):1211-6. PMID:10684598

1. ↑ 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
2. ↑ 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