4x1b
From Proteopedia
Human serum transferrin with ferric ion bound at the C-lobe only
Structural highlights
DiseaseTRFE_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] FunctionTRFE_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. Publication Abstract from PubMedX-ray crystal structures of human serum transferrin (77 kDa) with YbIII or FeIII bound to the C-lobe and malonate as the synergistic anion show that the large YbIII ion causes the expansion of the metal binding pocket while octahedral metal coordination geometry is preserved, an unusual geometry for a lanthanide ion. "Anion clamp" allows flexible protein to impose coordination geometry on metal ions.,Wang M, Lai TP, Wang L, Zhang H, Yang N, Sadler PJ, Sun H Chem Commun (Camb). 2015 Apr 9. PMID:25854324[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Homo sapiens | Large Structures | Sun H | Wang M | Zhang H
