Sandbox GGC8
From Proteopedia
(Difference between revisions)
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| - | ==Hemoglobin A | + | ==Hemoglobin A== |
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene='78/781194/87_-58_his/1'> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene='78/781194/87_-58_his/1'> | ||
| - | This is a default text for your page '''Sandbox GGC8'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
| - | <scene name='78/781194/92-63/2'>This scene show the relative orientation of the proximal His87 and the distal His 58</scene> | ||
| - | <scene name='78/781194/Hemoglobin/1'>This scene show the structure of the full hemoglobin </scene> | ||
| - | <scene name='78/781194/92-63/3'>this scene show the proximal 92 His and distal 63 His </scene> | ||
| - | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
== Function == | == Function == | ||
| - | The function of Hemoglobin is to carry oxygen from the lungs to the other parts of the body . Hemoglobin also help to carry carbon dioxide through the blood cells.Hemoglobin A which is a component of the red blood cells also help with the transportation of carbon dioxide and hydrogen ions to the lungs. Hemoglobin proteins are capable of carrying four molecules of Oxygen . Hemoglobin also help red blood cells to maintain their disc like shape , which allows them to move freely through the blood vessels. | + | Hemoglobin A is an oxygen-transport protein. Hemoglobin is also an allosteric protein. It is a tetrameter composed of two types of sub units designated α and β, with stoichiometry α2β2 |
| + | The function of Hemoglobin is to carry oxygen from the lungs to the other parts of the body . Hemoglobin also help to carry carbon dioxide through the blood cells.Hemoglobin A which is a component of the red blood cells also help with the transportation of carbon dioxide and hydrogen ions to the lungs. Hemoglobin proteins are capable of carrying four molecules of Oxygen . Hemoglobin also help red blood cells to maintain their disc like shape , which allows them to move freely through the blood vessels. Each sub-unit of Hemoglobin A contains a heme prosthetic group. The heme molecules give hemoglobin its red color. | ||
== Disease == | == Disease == | ||
| - | + | The most well-known disease caused by a mutation in the hemoglobin A protein is sickle-cell anemia. Sickle-cell anemia results from a mutation of the sixth residue in the β hemoglobin monomer from glutamic acid to a valine. This hemoglobin variant is termed 'hemoglobin S' (2hbs). | |
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== Relevance == | == Relevance == | ||
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== Structural highlights == | == Structural highlights == | ||
| + | <scene name='78/781194/92-63/2'>This scene show the relative orientation of the proximal His87 and the distal His 58</scene> | ||
| + | <scene name='78/781194/Hemoglobin/1'>This scene show the structure of the full hemoglobin </scene> | ||
| + | <scene name='78/781194/92-63/3'>this scene show the proximal 92 His and distal 63 His </scene> | ||
| + | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
| + | |||
The first structure is a ball stick representing the approximate distance distance between two His 87 proximal and His distal 58 from the hemoglobin structure. The second scene consist of a full sturcture of the hemoglobin and all of its components. The third scene is From the Beta chain of the hemoglobin it is showing the distance from the proximal His 92 to the distal His 63 . | The first structure is a ball stick representing the approximate distance distance between two His 87 proximal and His distal 58 from the hemoglobin structure. The second scene consist of a full sturcture of the hemoglobin and all of its components. The third scene is From the Beta chain of the hemoglobin it is showing the distance from the proximal His 92 to the distal His 63 . | ||
Revision as of 14:36, 19 November 2019
Hemoglobin A
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References
Crystal structure of Lysβ182-Lysβ282 crosslinked hemoglobin: A possible allosteric intermediate1 https://www.sciencedirect.com/science/article/pii/S0022283600935253?via%3Dihub#FIG4
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
