4wjg | pdb_00004wjg

Structure of T. brucei haptoglobin-hemoglobin receptor binding to human haptoglobin-hemoglobin

spinqualitylabelsall models 4wjg, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wjg is a 30 chain structure with sequence from Homo sapiens, Staphylococcus aureus subsp. aureus N315 and Trypanosoma brucei brucei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.1Å Ligands: HEM, NAG, OXY Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ISDH_STAAN Binds human plasma haptoglobin-hemoglobin complexes, haptoglobin and hemoglobin. Binds haptoglobin-hemoglobin complexes with significantly higher affinity than haptoglobin alone (By similarity). Publication Abstract from PubMed Sleeping sickness is caused by trypanosome parasites, which infect humans and livestock in Sub-Saharan Africa. Haem is an important growth factor for the parasites and is acquired from the host by receptor-mediated uptake of haptoglobin (Hp)-haemoglobin (Hb) complexes. The parasite Hp-Hb receptor (HpHbR) is also a target for a specialized innate immune defence executed by trypanosome-killing lipoprotein particles containing an Hp-related protein in complex with Hb. Here we report the structure of the multimeric complex between human Hp-Hb and Trypanosoma brucei brucei HpHbR. Two receptors forming kinked three-helical rods with small head regions bind to Hp and the beta-subunits of Hb (betaHb), with one receptor at each end of the dimeric Hp-Hb complex. The Hb beta-subunit haem group directly associates with the receptors, which allows for sensing of haem-containing Hp-Hb. The HpHbR-binding region of Hp is conserved in Hp-related protein, indicating an identical recognition of Hp-Hb and trypanolytic particles by HpHbR in human plasma. Structural basis for trypanosomal haem acquisition and susceptibility to the host innate immune system.,Stodkilde K, Torvund-Jensen M, Moestrup SK, Andersen CB Nat Commun. 2014 Nov 20;5:5487. doi: 10.1038/ncomms6487. PMID:25410714 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Haptoglobin receptor Hemoglobin 3D structures

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