9klt

Crystal structure of a Streptococcal protein G B1 mutant

spinqualitylabelsall models 9klt, resolution 2.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9klt is a 1 chain structure with sequence from Finegoldia magna. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.88Å Ligands: EPE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q53291_FINMA Publication Abstract from PubMed Homobivalent small binders represent bioactive dimeric proteins constructed by linking nanobodies or other small binders. As binding domain orientation in these dimeric binders affects binding affinity, expanding the orientation regulation techniques is crucial for optimizing their performance. Here, we report a 3D domain-swapping design as a genetic engineering approach to regulate the orientation of homobivalent small binders. We aimed to regulate B1 domain orientation of protein G as a model binder. By inserting single cysteine-containing polyproline sequences into loops located at the C- and N-terminal sides of the tertiary structure, we successfully designed 3D domain-swapped dimers with tail-to-tail and head-to-head orientations. Notably, the head-to-head-oriented dimer demonstrated potential as a functional homobivalent small binder. Our results highlight the applicability of the 3D domain-swapping design for regulating the orientation of homobivalent small binders and establish a foundation for developing 3D domain-swapped dimers. Regulating the orientation of homobivalent small binders through 3D domain-swapping design.,Shiga S, Watanabe H, Makabe K, Honda S J Biol Chem. 2025 Dec 13;302(2):111053. doi: 10.1016/j.jbc.2025.111053. PMID:41391770 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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