Structural highlights
Function
HBA_HORSE Involved in oxygen transport from the lung to the various peripheral tissues.
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
A new relaxed state has been characterized in the crystals of horse methemoglobin grown at neutral pH at low ionic concentration and their low humidity variants. The crystals provide an example for improvement in X-ray diffraction quality with reduced solvent content. Only the classical R state has been so far observed in liganded horse hemoglobin. The state characterized in the present study lies in between the R state and the R2 state characterized earlier in liganded human hemoglobin. The results presented here, along with those of earlier studies, suggest that relaxed and tense hemoglobin can access ensembles of states.
A new relaxed state in horse methemoglobin characterized by crystallographic studies.,Sankaranarayanan R, Biswal BK, Vijayan M Proteins. 2005 Aug 15;60(3):547-51. PMID:15887226[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sankaranarayanan R, Biswal BK, Vijayan M. A new relaxed state in horse methemoglobin characterized by crystallographic studies. Proteins. 2005 Aug 15;60(3):547-51. PMID:15887226 doi:http://dx.doi.org/10.1002/prot.20510
