Sandbox GGC8
From Proteopedia
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== Function == | == Function == | ||
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 | 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. | + | 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.<ref>doi:10.1007/s10533-009-9387-8</ref> |
== Disease == | == Disease == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | <scene name='78/781194/92-63/2'> | + | <scene name='78/781194/92-63/2'>Proximal His87 and the distal His 58</scene> The α chain heme pocket with the relative orientation of the proximal Hisα87 and the distal Hisα58.proximal Hisα87(F8) is closer to the heme Fe atom by 0.10 Å more in the T-state compare to the R-state.<ref>doi: 10.1074/jbc.M109.066027</ref> |
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<scene name='78/781194/Hemoglobin/1'>This scene show the structure of the full hemoglobin </scene> | <scene name='78/781194/Hemoglobin/1'>This scene show the structure of the full hemoglobin </scene> | ||
| - | <scene name='78/781194/92-63/3'> | + | |
| + | <scene name='78/781194/92-63/3'>Proximal 92 His and distal 63 His </scene>) The β chain heme pocket with the proximal Hisβ92(F8) and the distal Hisβ63(E7). In the R-state the proximal Hisβ92(F8) reorients itself to a more symmetric position relative to the heme molecule. In the T-state, the distal histidine E7 residue is positioned such that it partially blocks the oxygen-binding site. During the R → T transition, Hisβ63(E7) aligns itself with the heme Fe, and the Fe-His distances increase by a small but detectable amount<ref>doi: 10.1074/jbc.M109.066027</ref> | ||
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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. | 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 . | ||
| - | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
</StructureSection> | </StructureSection> | ||
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https://www.sciencedirect.com/science/article/pii/S0022283600935253?via%3Dihub#FIG4 | https://www.sciencedirect.com/science/article/pii/S0022283600935253?via%3Dihub#FIG4 | ||
<references/> | <references/> | ||
| + | https://www.verywellhealth.com/importance-of-hemoglobin-2249107 | ||
Revision as of 21:04, 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
- ↑ doi: https://dx.doi.org/10.1007/s10533-009-9387-8
- ↑ Rothery RA, Bertero MG, Spreter T, Bouromand N, Strynadka NC, Weiner JH. Protein crystallography reveals a role for the FS0 cluster of Escherichia coli nitrate reductase A (NarGHI) in enzyme maturation. J Biol Chem. 2010 Mar 19;285(12):8801-7. Epub 2010 Jan 6. PMID:20053990 doi:10.1074/jbc.M109.066027
- ↑ Rothery RA, Bertero MG, Spreter T, Bouromand N, Strynadka NC, Weiner JH. Protein crystallography reveals a role for the FS0 cluster of Escherichia coli nitrate reductase A (NarGHI) in enzyme maturation. J Biol Chem. 2010 Mar 19;285(12):8801-7. Epub 2010 Jan 6. PMID:20053990 doi:10.1074/jbc.M109.066027
- ↑ 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
https://www.verywellhealth.com/importance-of-hemoglobin-2249107
