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5XCX

Crystal structure of TS2/16 Fv-clasp fragment

Summary for 5XCX
Entry DOI10.2210/pdb5xcx/pdb
Related5XCQ 5XCR 5XCS 5XCT 5XCU 5XCV
DescriptorVH(S112C)-SARAH Chimera, VL-SARAH(S37C) Chimera, PHOSPHATE ION, ... (6 entities in total)
Functional Keywordsantibody fragment, fv-clasp, immune system
Biological sourceMus musculus
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Total number of polymer chains2
Total formula weight38554.37
Authors
Arimori, T.,Takagi, J. (deposition date: 2017-03-23, release date: 2017-10-04, Last modification date: 2024-10-30)
Primary citationArimori, 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: 28919443
DOI: 10.1016/j.str.2017.08.011
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.04 Å)
Structure validation

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数据于2024-11-06公开中

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