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| | <StructureSection load='4nxc' size='340' side='right'caption='[[4nxc]], [[Resolution|resolution]] 1.55Å' scene=''> | | <StructureSection load='4nxc' size='340' side='right'caption='[[4nxc]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4nxc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NXC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NXC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4nxc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NXC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=N2O:NITROUS+OXIDE'>N2O</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=N2O:NITROUS+OXIDE'>N2O</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4nxa|4nxa]], [[4o4z|4o4z]], [[4o4t|4o4t]], [[4nwh|4nwh]], [[4nwe|4nwe]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nxc OCA], [https://pdbe.org/4nxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nxc RCSB], [https://www.ebi.ac.uk/pdbsum/4nxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nxc ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nxc OCA], [http://pdbe.org/4nxc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nxc RCSB], [http://www.ebi.ac.uk/pdbsum/4nxc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nxc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MYG_PHYCD MYG_PHYCD]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | + | [https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Myoglobin|Myoglobin]] | + | *[[Myoglobin 3D structures|Myoglobin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Physeter catodon]] | | [[Category: Physeter catodon]] |
| - | [[Category: Prange, T]] | + | [[Category: Colloc'h N]] |
| - | [[Category: Vallone, B]]
| + | [[Category: Prange T]] |
| - | [[Category: H, N Colloc]]
| + | [[Category: Vallone B]] |
| - | [[Category: Globin]] | + | |
| - | [[Category: Oxygen transport]] | + | |
| Structural highlights
Function
MYG_PHYMC Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
Publication Abstract from PubMed
BACKGROUND:: The mechanisms by which general anesthetics, including xenon and nitrous oxide, act are only beginning to be discovered. However, structural approaches revealed weak but specific protein-gas interactions. METHODS:: To improve knowledge, we performed x-ray crystallography studies under xenon and nitrous oxide pressure in a series of 10 binding sites within four proteins. RESULTS:: Whatever the pressure, we show (1) hydrophobicity of the gas binding sites has a screening effect on xenon and nitrous oxide binding, with a threshold value of 83% beyond which and below which xenon and nitrous oxide, respectively, binds to their sites preferentially compared to each other; (2) xenon and nitrous oxide occupancies are significantly correlated respectively to the product and the ratio of hydrophobicity by volume, indicating that hydrophobicity and volume are binding parameters that complement and oppose each other's effects; and (3) the ratio of occupancy of xenon to nitrous oxide is significantly correlated to hydrophobicity of their binding sites. CONCLUSIONS:: These data demonstrate that xenon and nitrous oxide obey different binding mechanisms, a finding that argues against all unitary hypotheses of narcosis and anesthesia, and indicate that the Meyer-Overton rule of a high correlation between anesthetic potency and solubility in lipids of general anesthetics is often overinterpreted. This study provides evidence that the mechanisms of gas binding to proteins and therefore of general anesthesia should be considered as the result of a fully reversible interaction between a drug ligand and a receptor as this occurs in classical pharmacology.
Crystallographic Studies with Xenon and Nitrous Oxide Provide Evidence for Protein-dependent Processes in the Mechanisms of General Anesthesia.,Abraini JH, Marassio G, David HN, Vallone B, Prange T, Colloc'h N Anesthesiology. 2014 Sep 10. PMID:25211169[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Abraini JH, Marassio G, David HN, Vallone B, Prange T, Colloc'h N. Crystallographic Studies with Xenon and Nitrous Oxide Provide Evidence for Protein-dependent Processes in the Mechanisms of General Anesthesia. Anesthesiology. 2014 Sep 10. PMID:25211169 doi:http://dx.doi.org/10.1097/ALN.0000000000000435
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