Structural highlights
Function
HBAZ_HUMAN The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin, synthesized primarily in the yolk sac.
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
By using transgenic methodologies, we have produced a number of mouse/human chimeric hemoglobins containing adult mouse and human embryonic globin chains. A detailed analysis of the oxygen binding properties of these proteins identifies the dominant role played by the specific beta-type globin chains in the control of the oxygen binding characteristics. Further analysis traces the origins of these effects to alterations in the properties of the T states of these proteins. The human zeta/mouse beta chimeric protein has been crystallized, and its structure has been determined by X-ray diffraction to a resolution of 2.1 A with R (R(free)) values of 21.6% (24.9%). Close examination of the structure indicates that the subunit interfaces contain contacts which, although different from those present in either the parent human or the parent mouse proteins, retain the overall stabilizing interactions seen in other R state hemoglobins.
The role of beta chains in the control of the hemoglobin oxygen binding function: chimeric human/mouse proteins, structure, and function.,Kidd RD, Russell JE, Watmough NJ, Baker EN, Brittain T Biochemistry. 2001 Dec 25;40(51):15669-75. PMID:11747442[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kidd RD, Russell JE, Watmough NJ, Baker EN, Brittain T. The role of beta chains in the control of the hemoglobin oxygen binding function: chimeric human/mouse proteins, structure, and function. Biochemistry. 2001 Dec 25;40(51):15669-75. PMID:11747442
