Structural highlights
Function
[CYGB_HUMAN] May have a protective function during conditions of oxidative stress. May be involved in intracellular oxygen storage or transfer.
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
Cytoglobin (Cgb) is a recently discovered member of the vertebrate haem-containing globin family. The structure of a new crystal form of wild-type human Cgb (space group C2) was determined at a resolution of 1.68 Angstrom. The results show the presence of an additional helix in the N-terminal residues (4-20) prior to the A helix and an ordered loop structure in the C-terminal region (168-188), while these extended peptides were invisible owing to disorder in the previously reported structures using a P3(2)21 crystal at a resolution of 2.4 Angstrom. A detailed comparison of the two crystal structures shows differences in the conformation of the residues (i.e. Arg84) in the haem environment owing to a different dimeric arrangement.
High-resolution structure of human cytoglobin: identification of extra N- and C-termini and a new dimerization mode.,Makino M, Sugimoto H, Sawai H, Kawada N, Yoshizato K, Shiro Y Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):671-7. Epub 2006, May 12. PMID:16699195[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Makino M, Sugimoto H, Sawai H, Kawada N, Yoshizato K, Shiro Y. High-resolution structure of human cytoglobin: identification of extra N- and C-termini and a new dimerization mode. Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):671-7. Epub 2006, May 12. PMID:16699195 doi:10.1107/S0907444906013813
