Structural highlights
Function
SAV_STRAV The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).
Publication Abstract from PubMed
We previously created a low-immunogenic core streptavidin mutant No. 314 (LISA-314) by replacing six amino-acid residues for use as a delivery tool for an antibody multistep pre-targeting process (Yumura et al., Protein science, 22, 213-221, 2013). Here, we performed high-resolution X-ray structural analyses of LISA-314 and wild-type streptavidin to investigate the effect of substitutions on the protein function and the three-dimensional structure. LISA-314 forms a tetramer in the same manner as wild-type streptavidin. The binding mode of d-biotin in LISA-314 is also completely identical to that in wild-type streptavidin, and conformational changes were observed mostly at the side chains of substituted sites. Any large conformational changes corresponding to the reduction of B factors around the substituted sites were not observed. These results demonstrated the LISA-314 acquired low immunogenicity without losing structural properties of original wild-type streptavidin.
Crystal structure of streptavidin mutant with low immunogenicity.,Kawato T, Mizohata E, Meshizuka T, Doi H, Kawamura T, Matsumura H, Yumura K, Tsumoto K, Kodama T, Inoue T, Sugiyama A J Biosci Bioeng. 2014 Nov 26. pii: S1389-1723(14)00403-4. doi:, 10.1016/j.jbiosc.2014.10.025. PMID:25434833[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kawato T, Mizohata E, Meshizuka T, Doi H, Kawamura T, Matsumura H, Yumura K, Tsumoto K, Kodama T, Inoue T, Sugiyama A. Crystal structure of streptavidin mutant with low immunogenicity. J Biosci Bioeng. 2014 Nov 26. pii: S1389-1723(14)00403-4. doi:, 10.1016/j.jbiosc.2014.10.025. PMID:25434833 doi:http://dx.doi.org/10.1016/j.jbiosc.2014.10.025
