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7C61

Crystal structure of 5-HT1B-BRIL and SRP2070_Fab complex

Summary for 7C61
Entry DOI10.2210/pdb7c61/pdb
DescriptorIGG LIGHT CHAIN, IGG HEAVY CHAIN, 5-hydroxytryptamine receptor 1B,Soluble cytochrome b562,5-hydroxytryptamine receptor 1B, ... (4 entities in total)
Functional Keywordsgpcr, bril, crystallization, antibody, signaling protein
Biological sourceMus musculus
More
Total number of polymer chains3
Total formula weight104615.00
Authors
Suzuki, M.,Miyagi, H.,Asada, H.,Yasunaga, M.,Suno, C.,Takahashi, Y.,Saito, J.,Iwata, S. (deposition date: 2020-05-21, release date: 2020-07-29, Last modification date: 2024-10-23)
Primary citationMiyagi, H.,Asada, H.,Suzuki, M.,Takahashi, Y.,Yasunaga, M.,Suno, C.,Iwata, S.,Saito, J.I.
The discovery of a new antibody for BRIL-fused GPCR structure determination.
Sci Rep, 10:11669-11669, 2020
Cited by
PubMed Abstract: G-protein-coupled receptors (GPCRs)-the largest family of cell-surface membrane proteins-mediate the intracellular signal transduction of many external ligands. Thus, GPCRs have become important drug targets. X-ray crystal structures of GPCRs are very useful for structure-based drug design (SBDD). Herein, we produced a new antibody (SRP2070) targeting the thermostabilised apocytochrome b562 from Escherichia coli M7W/H102I/R106L (BRIL). We found that a fragment of this antibody (SRP2070Fab) facilitated the crystallisation of the BRIL-tagged, ligand bound GPCRs, 5HT and ATR. Furthermore, the electron densities of the ligands were resolved, suggesting that SPR2070Fab is versatile and adaptable for GPCR SBDD. We anticipate that this new tool will significantly accelerate structure determination of other GPCRs and the design of small molecular drugs targeting them.
PubMed: 32669569
DOI: 10.1038/s41598-020-68355-x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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