7KNT: Apo-CGRP receptor in a detergent micelle

CryoEM structure of the apo-CGRP receptor in a detergent micelle. Determined by electron microscopy at 3.15 Å resolution. Released 24 Feb 2021.

Method: Electron microscopy
Resolution: 3.15 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,716
Mol. weight: 73.34 kDa
Released: 24 Feb 2021

Explore 7KNT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7KNT contains 27 α-helices and 10 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain E: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	30-39	10
α-helix	44-55	12
α-helix	63-80	18
α-helix	87-100	14
α-helix	119-141	23

Chain R: 22 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	34-53	20
β-strand	69	1	1
β-strand	74	1	1
β-strand	86-87	2	2
β-strand	100-101	2	2
β-strand	102	1	3
β-strand	105	1	4
β-strand	111	1	4
α-helix	112	1
β-strand	113	1	5
α-helix	114	1
β-strand	120	1	5
β-strand	123	1	3
α-helix	125-127	3
α-helix	133-146	14
α-helix	148-165	18
α-helix	173-197	25
α-helix	202-206	5
α-helix	210-238	29
α-helix	239-243	5
α-helix	254-256	3
α-helix	257-261	5
α-helix	264-276	13
α-helix	281-283	3
α-helix	289-291	3
α-helix	292-318	27
α-helix	330-339	10
α-helix	341-350	10
α-helix	364-374	11
α-helix	376-381	6
α-helix	382-386	5
α-helix	389-396	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Receptor activity-modifying protein 1	E	protein	149	Homo sapiens	O60894 (AlphaFold model)
Calcitonin gene-related peptide type 1 receptor	R	protein	490	Homo sapiens	Q16602 (AlphaFold model)

Sequence of entity 1 (E), FASTA

>7KNT_1 Receptor activity-modifying protein 1 (chains E)
MKTIIALSYIFCLVFADYKDDDDKHGSCQEANYGALLRELCLTQFQVDMEAVGETLWCDW
GRTIRSYRELADCTWHMAEKLGCFWPNAEVDRFFLAVHGRYFRSCPISGRAVRDPPGSIL
YPFIVVPITVTLLVTALVVWQSKRTEGIV

Sequence of entity 2 (R), FASTA

>7KNT_2 Calcitonin gene-related peptide type 1 receptor (chains R)
MKTIIALSYIFCLVFADYKDDDDLEVLFQGPAELEESPEDSIQLGVTRNKIMTAQYECYQ
KIMQDPIQQAEGVYCNRTWDGWLCWNDVAAGTESMQLCPDYFQDFDPSEKVTKICDQDGN
WFRHPASNRTWTNYTQCNVNTHEKVKTALNLFYLTIIGHGLSIASLLISLGIFFYFKSLS
CQRITLHKNLFFSFVCNSVVTIIHLTAVANNQALVATNPVSCKVSQFIHLYLMGCNYFWM
LCEGIYLHTLIVVAVFAEKQHLMWYYFLGWGFPLIPACIHAIARSLYYNDNCWISSDTHL
LYIIHGPICAALLVNLFFLLNIVRVLITKLKVTHQAESNLYMKAVRATLILVPLLGIEFV
LIPWRPEGKIAEEVYDYIMHILMHFQGLLVSTIFCFFNGEVQAILRRNWNQYKIQFGNSF
SNSEALRSASYTVSTISDGPGYSHDCPSEHLNGKSIHDIENVLLKPENLYNPAGLEVLFQ
GPHHHHHHHH

Primary citation

Structure and dynamics of the CGRP receptor in apo and peptide-bound forms. Josephs, T.M., Belousoff, M.J., Liang, Y.L. et al. Science (2021) 372. DOI 10.1126/science.abf7258 · PubMed

Other PDB entries of the same protein (UniProt O60894 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6ZHO 1.6 Å, Crystal structure of a CGRP receptor ectodomain heterodimer with bound high affinity…
8AX7 1.65 Å, Crystal structure of a CGRP receptor ectodomain heterodimer bound to macrocyclic…
7P0F 1.85 Å, Crystal structure of a CGRP receptor ectodomain heterodimer bound to macrocyclic…
8AX6 1.9 Å, Crystal structure of a CGRP receptor ectodomain heterodimer bound to macrocyclic…
6D1U 2.05 Å, Crystal structure of the human CLR:RAMP1 extracellular domain heterodimer in complex…
3N7S 2.1 Å, Crystal structure of the ectodomain complex of the CGRP receptor, a Class-B GPCR,…
7TYF 2.2 Å, Human Amylin1 Receptor in complex with Gs and rat amylin peptide
9BP3 2.2 Å, Human Amylin1 Receptor in complex with Gs and cagrilintide
7P0I 2.3 Å, Crystal structure of a CGRP receptor ectodomain heterodimer bound to macrocyclic…
2YX8 2.4 Å, Crystal structure of the extracellular domain of human RAMP1
9AUC 2.4 Å, Human Amylin1 Receptor in Complex with Gs and human Calcitonin Gene-Related Peptide
4RWG 2.44 Å, Crystal structure of the CLR:RAMP1 extracellular domain heterodimer with bound high…

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