Cytoglobin: Difference between revisions
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==Cytoglobin== | ==Cytoglobin== | ||
<StructureSection load=' | <StructureSection load='2dc3' size='350' side='right' caption='Crystal Structure of Human Cytoglobin at 1.68 Angstroms Resolution' scene=''> | ||
== General Description == | == General Description == | ||
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== Structural Insights into Function == | == Structural Insights into Function == | ||
Cytoglobin’s structure, particularly the heme group, contributes to its function greatly. In the deoxygenated form of cytoglobin, the heme group is coordinated with endogenous ligands at all 6 sites of the heme group, with the 6th site being occupied by a distal Histidine (His E7) residue on the protein. Oxygen competes with this His residue to bind CYGB<ref>https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4925767/</ref>. | Cytoglobin’s structure, particularly the heme group, contributes to its function greatly. In the deoxygenated form of cytoglobin, the heme group is coordinated with endogenous ligands at all 6 sites of the heme group, with the 6th site being occupied by a distal<scene name='74/748876/His_residues/1'> Histidine (His E7)</scene> residue on the protein. Oxygen competes with this His residue to bind CYGB<ref>https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4925767/</ref>. | ||
