1a9w | pdb_00001a9w

HUMAN EMBRYONIC GOWER II CARBONMONOXY HEMOGLOBIN

spinqualitylabelsall models 1a9w, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1a9w is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: CMO, HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HBE_HUMAN The epsilon chain is a beta-type chain of early mammalian embryonic hemoglobin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The production of recombinant embryonic haemoglobins via a yeast expression system has enabled structural and functional studies to be conducted on these proteins. As part of a programme aimed at understanding the properties of the embryonic haemoglobins we have crystallized the human alpha2 epsilon2 (Gower II) embryonic haemoglobin in its carbonmonoxy form, and determined its structure by X-ray crystallography. The structure was solved by molecular replacement and refined at 2.9 A to give a final model with R-factor=0.185 and Rfree=0.235. The Gower II hemoglobin tetramer is intermediate between the adult R and R2 states, though closer to R2. The tertiary structure of the conserved alpha subunit is essentially identical when compared to that found in the adult (alpha2 beta2) and fetal (alpha2 gamma2) hemoglobins. The embryonic epsilon subunit has a structure very similar to that of the homologous adult beta and fetal gamma subunits, although with small differences at the N terminus and in the A helix. Amino acid substitutions can be identified that may play a role in the altered response of the Gower II haemoglobin to allosteric effectors, in particular chloride ions. The reduced chloride effect is thought to be the primary cause of the higher affinity of this embryonic hemoglobin in comparison to the adult molecule. Crystal structure of a human embryonic haemoglobin: the carbonmonoxy form of gower II (alpha2 epsilon2) haemoglobin at 2.9 A resolution.,Sutherland-Smith AJ, Baker HM, Hofmann OM, Brittain T, Baker EN J Mol Biol. 1998 Jul 17;280(3):475-84. PMID:9665850 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hemoglobin 3D structures

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