3wyq

<StructureSection load='3wyq' size='340' side='right'caption='[[3wyq]], [[Resolution|resolution]] 1.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[3wyq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WYQ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3wyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wyq OCA], [https://pdbe.org/3wyq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wyq RCSB], [https://www.ebi.ac.uk/pdbsum/3wyq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wyq ProSAT]</span></td></tr>

== Function ==

[[https://www.uniprot.org/uniprot/SAV_STRAV 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).

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== 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<ref>PMID:25434833</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3wyq" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Doi, H]]

[[Category: Inoue, T]]

[[Category: Kawamura, T]]

[[Category: Kawato, T]]

[[Category: Kodama, T]]

[[Category: Matsumura, H]]

[[Category: Meshizuka, T]]

[[Category: Mizohata, E]]

[[Category: Sugiyama, A]]

[[Category: Tsumoto, K]]

[[Category: Yumura, K]]

[[Category: Biotin binding protein]]