Neuroglobin

Neuroglobin is mainly expressed in vertebrate brain and retina. It binds oxygen and has a fold very similar to myoglobin.

Both neuroglobin and myoglobin have hexa-coordinated Fe, unlike myoglobin and hemoglobin, which have an open site (penta-coordinated). Look for 2 cpk-colored histidines to appear in each protein, which coordinate the heme-Fe.



Pesce, A., Dewilde, S., Nardini, M., Moens, L., Ascenzi, P., Hankeln, T., Burmester, T., Bolognesi, M.: Human Brain Neuroglobin Structure Reveals a Distinct Mode of Controlling Oxygen Affinity Structure 11 pp. 1087 (2003)
(PubMed)

1oj6 (PDB)

Cytoglobin

Cytoglobin is found in many tissues, and can also bind oxygen, carbon monoxide and nitric oxide. Human cytoglobin has 190 aa residues. A core region (about 150 residues, shown here) is structurally related to hemoglobin and myoglobin, with about 20 extra residues at both termini.

The roles of these proteins are not well-understood. They were only discovered in about 2000.


De Sanctis, D., Dewilde, S., Pesce, A., Moens, L., Ascenzi, P., Hankeln, T., Burmester, T., Bolognesi, M.: Crystal Structure of Cytoglobin: The Fourth Globin Type Discovered in Man Displays Heme Hexa-Coordination J.Mol.Biol. 336 pp. 917 (2004)
(PubMed)

1urv (PDB)