Myoglobin
Encyclopedia : M : MY : MYO : Myoglobin
| Myoglobin | |
|---|---|
 Model of helical domains in myoglobin. | |
| Gene code: | HUGO code: MB |
| Structure: | [molecular structure] |
| Recent publications: | [role in human pathologies], [gene knockout] |
| protein type: | Hemoprotein |
| Functions: | oxygen storage/transport |
| Domains: | globin |
| Diseases: | kidney disease, vasospasm |
| Taxa expressing: | many metazoan phyla,Arhaea? protozoan/eubacterial? |
| Cell types: | muscle cells |
| Subcellular localization: | cytoplasm |
| covalent modifications | glycation?phosphorylation in whales? |
| Other names: | myoglobin-like proteins in microorganisms |
| Molecular interactions | oxygen,heme,carbon monoxide,nitric oxide |
| related articles: | X-ray crystallography,Secondary structure |
Myoglobin is a single-chain protein of 153 amino acids, containing a heme (iron-containing porphyrin) group in the center. With a molecular weight of 16,700 Daltons, it is the primary oxygen-carrying pigment of muscle tissues. Unlike the blood-borne hemoglobin, to which it is structurally related, this protein does not exhibit cooperative binding of oxygen. Instead, the binding of oxygen by myoglobin is unaffected by the oxygen pressure in the surrounding tissue. In 1957, John Kendrew and associates successfully determined the structure of myoglobin by high-resolution X-ray crystallographyOxy-myoglobin at 0.1 nm resolution: PDB [1A6M]. Sperm whale myoglobin at 0.17 nm resolution: PDB [1VXH]..
For this discovery, John Kendrew shared the 1962 Nobel Prize in chemistry with Max Perutz[The Nobel Prize in Chemistry 1962].
Role in disease
Myoglobin has been implicated as a cause of acute renal failure following damage to muscle tissue (e.g. rhabdomyolysis, severe crush trauma, malignant hyperthermia, status epilepticus and neuroleptic malignant syndrome), due to its toxicity to renal tubular epithelium.Myoglobin is a sensitive marker for muscle injury, making it a potential marker for myocardial infarction in patients with chest pain. Its specificity and the cost of the analysis has prevented its widespread use.
During muscle death due to infarction, myoglobin is released, which is toxic to the kidneys. If it is misdiagnosed, it can cause much worse conditions, such as cardiac arrest.
References
See also
External links
- [Protein Database featured molecule]
- OMIM [160000] human genetics
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