3pel | pdb_00003pel

Structure of Greyhound Hemoglobin: Origin of High Oxygen Affinity

spinqualitylabelsall models 3pel, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pel is a 2 chain structure with sequence from Canis lupus familiaris. This structure supersedes the now removed PDB entry 3n48. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HBA_CANLF Involved in oxygen transport from the lung to the various peripheral tissues. Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling.[UniProtKB:P01946] Publication Abstract from PubMed This study presents the crystal structure of Greyhound hemoglobin (GrHb) determined to 1.9 A resolution. GrHb was found to crystallize with an alpha(1)beta(1) dimer in the asymmetric unit and belongs to the R2 state. Oxygen-affinity measurements combined with the fact that GrHb crystallizes in the R2 state despite the high-salt conditions used for crystallization strongly indicate that GrHb can serve as a model high-oxygen-affinity hemoglobin (Hb) for higher mammals, especially humans. Structural analysis of GrHb and its comparison with the R2-state of human Hb revealed several regions that can potentially contribute to the high oxygen affinity of GrHb and serve to rationalize the additional stability of the R2-state of GrHb. A previously well studied hydrophobic cluster of bar-headed goose Hb near alpha119 was also incorporated in the comparison between GrHb and human Hb. Finally, a structural comparison with generic dog Hb and maned wolf Hb was conducted, revealing that in contrast to GrHb these structures belong to the R state of Hb and raising the intriguing possibility of an additional allosteric factor co-purifying with GrHb that can modulate its quaternary structure. Structure of Greyhound hemoglobin: origin of high oxygen affinity.,Bhatt VS, Zaldivar-Lopez S, Harris DR, Couto CG, Wang PG, Palmer AF Acta Crystallogr D Biol Crystallogr. 2011 May;67(Pt 5):395-402. Epub 2011, Apr 13. PMID:21543841 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hemoglobin 3D structures

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