3wyo
From Proteopedia
Heterodimeric 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. Loading citation details.. Citations No citations found See AlsoReferences
|
| |||||||||||||||||||
Categories: Equus caballus | Large Structures | Higuchi Y | Hirota S | Lin YW | Nagao S | Shomura Y | Zhang M
