7P0I
Crystal structure of a CGRP receptor ectodomain heterodimer bound to macrocyclic inhibitor Compound 13
Summary for 7P0I
Entry DOI | 10.2210/pdb7p0i/pdb |
Related | 7P0F |
Related PRD ID | PRD_900001 |
Descriptor | Maltose/maltodextrin-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, TETRAETHYLENE GLYCOL, ... (5 entities in total) |
Functional Keywords | gpcr, cgrp, ectodomain, inhibitor, macrocycle, membrane protein |
Biological source | Escherichia coli (strain K12) More |
Total number of polymer chains | 1 |
Total formula weight | 67698.96 |
Authors | Southall, S.M. (deposition date: 2021-06-29, release date: 2022-06-15, Last modification date: 2024-11-20) |
Primary citation | Cansfield, A.D.,Ator, M.A.,Banerjee, J.,Bestwick, M.,Bortolato, A.,Brown, G.A.,Brown, J.,Butkovic, K.,Cansfield, J.E.,Christopher, J.A.,Congreve, M.,Cseke, G.,Deflorian, F.,Dugan, B.,Hunjadi, M.P.,Hutinec, A.,Inturi, T.K.,Landek, G.,Mason, J.,O'Brien, A.,Ott, G.R.,Rupcic, R.,Saxty, G.,Southall, S.M.,Zadravec, R.,Watson, S.P. Novel Macrocyclic Antagonists of the Calcitonin Gene-Related Peptide Receptor: Design, Realization, and Structural Characterization of Protein-Ligand Complexes. Acs Chem Neurosci, 13:751-765, 2022 Cited by PubMed Abstract: A series of macrocyclic calcitonin gene-related peptide (CGRP) receptor antagonists identified using structure-based design principles, exemplified by HTL0028016 () and HTL0028125 (), is described. Structural characterization by X-ray crystallography of the interaction of two of the macrocycle antagonists with the CGRP receptor ectodomain is described, along with structure-activity relationships associated with point changes to the macrocyclic antagonists. The identification of non-peptidic/natural product-derived, macrocyclic ligands for a G protein coupled receptor (GPCR) is noteworthy. PubMed: 35245037DOI: 10.1021/acschemneuro.1c00696 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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