3wyo: Difference between revisions
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==Heterodimeric myoglobin formed by domain swapping== | ==Heterodimeric myoglobin formed by domain swapping== | ||
<StructureSection load='3wyo' size='340' side='right' caption='[[3wyo]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3wyo' size='340' side='right'caption='[[3wyo]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3wyo]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WYO OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[3wyo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WYO FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id=' | <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></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wyo OCA], [https://pdbe.org/3wyo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wyo RCSB], [https://www.ebi.ac.uk/pdbsum/3wyo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wyo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE] 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 == | ||
| Line 17: | Line 18: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3wyo" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Myoglobin 3D structures|Myoglobin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Equus caballus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Higuchi Y]] | ||
[[Category: | [[Category: Hirota S]] | ||
[[Category: | [[Category: Lin YW]] | ||
[[Category: | [[Category: Nagao S]] | ||
[[Category: | [[Category: Shomura Y]] | ||
[[Category: | [[Category: Zhang M]] | ||
Latest revision as of 16:34, 8 November 2023
Heterodimeric myoglobin formed by domain swappingHeterodimeric myoglobin formed by domain swapping
Structural highlights
FunctionMYG_HORSE Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Publication Abstract from PubMedProtein design is a useful method to create novel artificial proteins. A rational approach to design a heterodimeric protein using domain swapping for horse myoglobin (Mb) was developed. As confirmed by X-ray crystallographic analysis, a heterodimeric Mb with two different active sites was produced efficiently from two surface mutants of Mb, in which the charges of two amino acids involved in the dimer salt bridges were reversed in each mutant individually, with the active site of one mutant modified. This study shows that the method of constructing heterodimeric Mb with domain swapping is useful for designing artificial multiheme proteins. Rational Design of Heterodimeric Protein using Domain Swapping for Myoglobin.,Lin YW, Nagao S, Zhang M, Shomura Y, Higuchi Y, Hirota S Angew Chem Int Ed Engl. 2014 Nov 4. doi: 10.1002/anie.201409267. PMID:25370865[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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