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3WYP

Crystal structure of wild-type core streptavidin in complex with D-biotin/biotin-D-sulfoxide at 1.3 A resolution

3WYP の概要
エントリーDOI10.2210/pdb3wyp/pdb
関連するPDBエントリー3WYQ
分子名称Streptavidin, BIOTIN, GLYCEROL, ... (6 entities in total)
機能のキーワードbeta-barrel, biotin binding protein
由来する生物種Streptomyces avidinii
細胞内の位置Secreted: P22629
タンパク質・核酸の鎖数4
化学式量合計55247.65
構造登録者
Kawato, T.,Mizohata, E.,Meshizuka, T.,Doi, H.,Kawamura, T.,Matsumura, H.,Yumura, K.,Tsumoto, K.,Kodama, T.,Inoue, T.,Sugiyama, A. (登録日: 2014-09-05, 公開日: 2014-12-24, 最終更新日: 2023-11-08)
主引用文献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., 119:642-647, 2015
Cited by
PubMed Abstract: 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 Sci., 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.
PubMed: 25434833
DOI: 10.1016/j.jbiosc.2014.10.025
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.3 Å)
構造検証レポート
Validation report summary of 3wyp
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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