5XCU
Crystal structure of 12CA5 Fv-clasp fragment with its antigen peptide
Summary for 5XCU
Entry DOI | 10.2210/pdb5xcu/pdb |
Related | 5XCQ 5XCR 5XCS 5XCT 5XCV 5XCX |
Descriptor | VH(S112C)-SARAH chimera,VH(S112C)-SARAH chimera, VL-SARAH(S37C) chimera,VL-SARAH(S37C) chimera, HA peptide, ... (5 entities in total) |
Functional Keywords | antibody fragment, fv-clasp, immune system |
Biological source | Mus musculus More |
Total number of polymer chains | 6 |
Total formula weight | 78990.76 |
Authors | Arimori, T.,Takagi, J. (deposition date: 2017-03-23, release date: 2017-10-04, Last modification date: 2024-10-09) |
Primary citation | Arimori, T.,Kitago, Y.,Umitsu, M.,Fujii, Y.,Asaki, R.,Tamura-Kawakami, K.,Takagi, J. Fv-clasp: An Artificially Designed Small Antibody Fragment with Improved Production Compatibility, Stability, and Crystallizability Structure, 25:1611-1622.e4, 2017 Cited by PubMed Abstract: Antibody fragments are frequently used as a "crystallization chaperone" to aid structural analysis of complex macromolecules that are otherwise crystallization resistant, but conventional fragment formats have not been designed for this particular application. By fusing an anti-parallel coiled-coil structure derived from the SARAH domain of human Mst1 kinase to the variable region of an antibody, we succeeded in creating a novel chimeric antibody fragment of ∼37 kDa, termed "Fv-clasp," which exhibits excellent crystallization compatibility while maintaining the binding ability of the original IgG molecule. The "clasp" and the engineered disulfide bond at the bottom of the Fv suppressed the internal mobility of the fragment and shielded hydrophobic residues, likely contributing to the high heat stability and the crystallizability of the Fv-clasp. Finally, Fv-clasp antibodies showed superior "chaperoning" activity over conventional Fab fragments, and facilitated the structure determination of an ectodomain fragment of integrin α6β1. PubMed: 28919443DOI: 10.1016/j.str.2017.08.011 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.454 Å) |
Structure validation
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