Structural highlights
Function
[HBA_EQUAS] 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
Haemoglobin from donkey was purified and crystallized in space group C2. The present donkey haemoglobin model comprises of two subunits alpha and beta. These alpha and beta subunits comprise of 141 and 146 amino acid residues, respectively, and the haem groups. The donkey haemoglobin differs from horse only in two amino acids of alpha-chain (His20 to Asn and Tyr24 to Phe) and these substitutions do not significantly change the secondary structural features of donkey haemoglobin. The haem group region and subunit contacts are closely resemble with that of horse methaemoglobin.
Crystal structure of haemoglobin from donkey (Equus asinus) at 3A resolution.,Balasundaresan D, Saraboji K, Ponnuswamy MN Biochimie. 2006 Jun;88(6):719-23. Epub 2006 Jan 26. PMID:16488065[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Balasundaresan D, Saraboji K, Ponnuswamy MN. Crystal structure of haemoglobin from donkey (Equus asinus) at 3A resolution. Biochimie. 2006 Jun;88(6):719-23. Epub 2006 Jan 26. PMID:16488065 doi:10.1016/j.biochi.2006.01.001
