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| ==Hemoglobin A== | | ==Your Heading Here (maybe something like 'Structure')== |
| <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene='78/781194/87_-58_his/1'> | | <StructureSection load='3VEV' size='340' side='right' caption='Caption for this structure' scene=''> |
| <scene name='78/781194/Deoxy_human_hemoglobin_a/4'>DEOXY HUMAN HEMOGLOBIN A</scene> | | This is a default text for your page '''Sandbox GGC8'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. |
| | 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. |
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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
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| 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>
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| == Disease == | | == Disease == |
| The most well-known disease caused by 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 == |
| Most of the understanding that of human physiology and pathology come from laboratory research that were performed on Hemoglobin<ref>doi: 10.1074/jbc.M109.066027</ref>
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| . Hemoglobin A is important for the body ;it helps the body to maintained a balanced amount of red blood cells.Low red blood cells in the body tissues can cause fatigue and weakness.
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| == Structural highlights ==
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| <scene name='78/781194/Hemoglobin/3'>The four Heme groups of Hemoglobin</scene>The hemoglobin molecule is composed of four polypeptide chains which are non covalently bound to each other . Each polypeptide chain consist of one Fe+ atom.<ref>doi: 10.1074/1BIJ.M109.066027</ref>
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| <scene name='78/781194/87_-58_his/8'>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='78/781194/92-63/5'>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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| | == Structural highlights == |
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| | 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. |
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| </StructureSection> | | </StructureSection> |
| == References == | | == References == |
| Crystal structure of Lysβ182-Lysβ282 crosslinked hemoglobin: A possible allosteric intermediate1
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| https://www.sciencedirect.com/science/article/pii/S0022283600935253?via%3Dihub#FIG4
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| <references/> | | <references/> |
| https://www.verywellhealth.com/importance-of-hemoglobin-2249107
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