7Z3Q: Leptin

Crystal structure of the human leptin:LepR-CRH2 encounter complex to 3.6 A resolution. Determined by X-ray diffraction at 3.62 Å resolution. Released 22 Mar 2023.

Method: X-ray diffraction
Resolution: 3.62 Å
Organism: Homo sapiens
Chains: 6
Atoms: 7,102
Mol. weight: 134.17 kDa
Released: 22 Mar 2023

Explore 7Z3Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7Z3Q contains 28 α-helices and 57 β-strands across 6 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 A: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	24-45	22
α-helix	72-87	16
α-helix	92-114	23
α-helix	142-160	19

Chain B: 4 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	435-438	4	1
β-strand	445-450	6	1
β-strand	461-468	8	2
β-strand	472	1	3
β-strand	484-486	3	2
β-strand	488-490	3	1
β-strand	495-500	6	1
β-strand	507	1	3
β-strand	509-516	8	2
β-strand	521-523	3	2
α-helix	524-526	3
β-strand	527-529	3	2
α-helix	531-534	4
β-strand	535	1	1
α-helix	537-540	4
β-strand	541-548	8	4
β-strand	553-559	7	4
β-strand	568-576	9	5
β-strand	584-588	5	5
β-strand	595-599	5	4
β-strand	607-615	9	5
α-helix	622-628	7
β-strand	629-630	2	5

Chain C: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	25-43	19
α-helix	68-71	4
α-helix	72-87	16
α-helix	92-114	23
α-helix	143-160	18

Chain D: 5 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	434-438	5	6
β-strand	445-449	5	6
α-helix	452-457	6
β-strand	461-468	8	7
β-strand	472	1	8
β-strand	484-486	3	7
β-strand	488-490	3	6
β-strand	496-500	5	6
β-strand	507	1	8
β-strand	509-516	8	7
β-strand	522-523	2	7
α-helix	524-526	3
β-strand	527-529	3	7
α-helix	531-534	4
β-strand	535	1	6
α-helix	537-540	4
β-strand	541-548	8	9
β-strand	553-559	7	9
β-strand	568-576	9	10
β-strand	584-588	5	10
β-strand	595-599	5	9
β-strand	607-615	9	10
α-helix	621-628	8
β-strand	629-630	2	10

Chain E: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	25-44	20
α-helix	69-71	3
α-helix	72-87	16
α-helix	92-114	23
α-helix	142-160	19

Chain F: 5 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	431-433	3
β-strand	434-438	5	11
β-strand	445-449	5	11
β-strand	461-468	8	12
β-strand	472	1	13
β-strand	484-486	3	12
β-strand	488-490	3	11
β-strand	496-500	5	11
β-strand	507	1	13
β-strand	509-517	9	12
β-strand	520-523	4	12
α-helix	524-526	3
β-strand	527-529	3	12
α-helix	531-534	4
β-strand	535	1	11
α-helix	537-540	4
β-strand	541-548	8	14
β-strand	553-559	7	14
β-strand	568-576	9	15
β-strand	584-588	5	15
β-strand	595-599	5	14
β-strand	607-615	9	15
α-helix	621-628	8
β-strand	629-630	2	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Leptin	A, C, E	protein	171	Homo sapiens	P41159 (AlphaFold model)
Leptin receptor	B, D, F	protein	232	Homo sapiens	P48357 (AlphaFold model)

Sequence of entity 1 (A, C, E), FASTA

>7Z3Q_1 Leptin (chains A, C, E)
AHHHHHHPGGPGSENLYFQGGSTGGVPIQKVQDDTKTLIKTIVTRINDISHTQSVSSKQK
VTGLDFIPGLHPILTLSKMDQTLAVYQQILTSMPSRNVIQISNDLENLRDLLHVLAFSKS
CHLPWASGLETLDSLGGVLEASGYSTEVVALSRLQGSLQDMLWQLDLSPGC

Sequence of entity 2 (B, D, F), FASTA

>7Z3Q_2 Leptin receptor (chains B, D, F)
AHHHHHHPGGPGSENLYFQGGSSGIDVNINISCETDGYLTKMTCRWSTSTIQSLAESTLQ
LRYHRSSLYCSDIPSIHPISEPKDCYLQSDGFYECIFQPIFLLSGYTMWIRIQHSLGSLD
SPPTCVLPDSVVKPLPPSSVKAEITINIGLLKISWEKPVFPENNLQFQIRYGLSGKEVQW
KMYEVYDAKSKSVSLPVPDLSAVYAVQVRCKRLDGLGYWSNWSNPAYTVVMD

Primary citation

Mechanism of receptor assembly via the pleiotropic adipokine Leptin. Tsirigotaki, A., Dansercoer, A., Verschueren, K.H.G. et al. Nat Struct Mol Biol (2023) 30:551-563. DOI 10.1038/s41594-023-00941-9 · PubMed

Other PDB entries of the same protein (UniProt P41159 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1AX8 2.4 Å, Human obesity protein, leptin
9PUO 3.1 Å, Neutralizing monoclonal antibody Fab fragment bound to leptin
8X85 3.58 Å, Structure of leptin-LepR dimer
8X81 3.77 Å, Structure of leptin-LepR trimer with a large gap
8X80 3.88 Å, Structure of leptin-LepR trimer with a small gap
8AVE 5.62 Å, Human leptin in complex with the human LEP-R ectodomain fused to a C-terminal trimeric…
8AVF 6.45 Å, Human leptin in complex with the human LEP-R ectodomain fused to a C-terminal trimeric…
8AVO 6.84 Å, Human leptin in complex with the human LEP-R ectodomain fused to a C-terminal trimeric…
8K6Z NMR structure of human leptin

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