8HPY: Human LGI1-ADAM22 complex

Crystal structure of human LGI1-ADAM22 complex. Determined by X-ray diffraction at 5.87 Å resolution. Released 13 Dec 2023.

Method: X-ray diffraction
Resolution: 5.87 Å
Organism: Homo sapiens
Chains: 4
Atoms: 15,962
Mol. weight: 231.69 kDa
Ligands: NAG, CA
Released: 13 Dec 2023

Explore 8HPY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8HPY contains 53 α-helices and 150 β-strands across 4 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: 20 helices, 33 β-strands

Element	Residues	Length	Sheet
β-strand	239-247	9	1
α-helix	249-254	6
α-helix	259-280	22
β-strand	283-292	10	1
α-helix	305-318	14
β-strand	326-330	5	1
α-helix	334-335	2
β-strand	341-343	3	1
β-strand	355-358	4	1
α-helix	363-377	15
α-helix	385-389	5
α-helix	416-427	12
α-helix	432-435	4
α-helix	436-438	3
α-helix	466-468	3
β-strand	474-475	2	2
β-strand	478-479	2	2
β-strand	492	1	3
β-strand	495	1	3
α-helix	497-498	2
β-strand	502-504	3	4
β-strand	511	1	5
β-strand	514-515	2	4
α-helix	523-526	4
β-strand	528	1	5
β-strand	529	1	6
α-helix	530	1
β-strand	534-535	2	7
β-strand	540-543	4	7
β-strand	546-548	3	7
α-helix	550-558	9
β-strand	564	1	8
α-helix	565-566	2
α-helix	567-576	10
β-strand	585	1	9
β-strand	590	1	9
α-helix	598-600	3
β-strand	602	1	8
β-strand	605	1	8
β-strand	616-628	13	8
β-strand	631-641	11	8
β-strand	647-648	2	8
β-strand	650	1	8
α-helix	651-652	2
β-strand	661-664	4	10
β-strand	667-670	4	10
α-helix	671-674	4
α-helix	687-690	4
β-strand	692-694	3	11
β-strand	695	1	6
β-strand	700-702	3	11
β-strand	706-707	2	12
β-strand	713-714	2	12

Chain B: 21 helices, 35 β-strands

Element	Residues	Length	Sheet
β-strand	239-247	9	23
α-helix	249-254	6
α-helix	259-281	23
β-strand	283-292	10	23
α-helix	305-318	14
β-strand	326-331	6	23
α-helix	334-335	2
β-strand	341-343	3	23
β-strand	355-359	5	23
α-helix	363-378	16
α-helix	385-389	5
α-helix	416-427	12
α-helix	432-435	4
α-helix	436-438	3
α-helix	463-466	4
β-strand	474-475	2	24
β-strand	478-479	2	24
β-strand	491	1	25
β-strand	496	1	25
α-helix	497-498	2
β-strand	502-504	3	26
β-strand	511	1	27
α-helix	512-513	2
β-strand	514-515	2	26
α-helix	523-526	4
β-strand	528	1	27
β-strand	529	1	28
α-helix	530	1
β-strand	534-535	2	29
β-strand	540-543	4	29
β-strand	546-548	3	29
α-helix	550-558	9
β-strand	564	1	30
α-helix	565-566	2
α-helix	567-576	10
β-strand	585	1	31
β-strand	589	1	16
β-strand	590	1	31
α-helix	595-600	6
β-strand	602	1	30
β-strand	605	1	30
β-strand	616-628	13	30
β-strand	631-641	11	30
β-strand	647-648	2	30
β-strand	650	1	30
α-helix	651-652	2
β-strand	655-658	4	32
β-strand	661-664	4	32
β-strand	667-670	4	32
α-helix	671-674	4
α-helix	688-690	3
β-strand	692-693	2	33
β-strand	695	1	28
β-strand	701-702	2	33
β-strand	706-707	2	34
β-strand	713-714	2	34

Chain D: 6 helices, 41 β-strands

Element	Residues	Length	Sheet
β-strand	46-48	3	13
β-strand	52-56	5	13
β-strand	71-75	5	13
α-helix	82-83	2
β-strand	95-99	5	13
β-strand	102	1	14
β-strand	119-123	5	13
β-strand	126	1	14
α-helix	132-134	3
β-strand	143-145	3	13
β-strand	167-169	3	13
β-strand	175-176	2	15
α-helix	179-190	12
β-strand	194-195	2	13
β-strand	199-202	4	15
β-strand	209-210	2	15
α-helix	211-213	3
β-strand	223-231	9	16
β-strand	238-244	7	17
β-strand	247-254	8	17
β-strand	259-264	6	17
β-strand	273-279	7	17
β-strand	286-290	5	18
β-strand	295-299	5	18
β-strand	307-311	5	18
β-strand	318-322	5	18
β-strand	332-339	8	19
β-strand	344-350	7	19
β-strand	357-362	6	19
β-strand	367-373	7	19
β-strand	379-388	10	20
β-strand	395-403	9	20
β-strand	409-414	6	20
β-strand	419-425	7	20
α-helix	426-427	2
β-strand	432-440	9	21
β-strand	443-450	8	21
β-strand	452-460	9	21
β-strand	465-474	10	21
β-strand	479-484	6	22
β-strand	487-492	6	22
α-helix	498	1
β-strand	499-504	6	22
β-strand	511-517	7	22
β-strand	525-529	5	16
β-strand	534-538	5	16
β-strand	546-553	8	16

Chain E: 6 helices, 41 β-strands

Element	Residues	Length	Sheet
β-strand	46-48	3	35
β-strand	52-56	5	35
β-strand	71-75	5	35
α-helix	82-83	2
β-strand	95-99	5	35
β-strand	102-103	2	36
β-strand	119-123	5	35
β-strand	126-127	2	36
α-helix	132-134	3
β-strand	143-145	3	35
β-strand	167-169	3	35
β-strand	175-176	2	37
α-helix	179-190	12
β-strand	194-195	2	35
β-strand	199-202	4	37
β-strand	209-210	2	37
α-helix	211-213	3
β-strand	222-232	11	38
β-strand	238-244	7	39
β-strand	247-254	8	39
β-strand	259-264	6	39
β-strand	274-279	6	39
β-strand	285-290	6	40
β-strand	295-300	6	40
β-strand	308-311	4	40
β-strand	318-322	5	40
β-strand	332-339	8	41
β-strand	344-350	7	41
β-strand	357-362	6	41
β-strand	367-373	7	41
β-strand	379-388	10	42
β-strand	395-403	9	42
β-strand	409-414	6	42
β-strand	419-425	7	42
α-helix	426	1
β-strand	432-440	9	43
β-strand	443-450	8	43
β-strand	452-460	9	43
β-strand	465-474	10	43
β-strand	479-484	6	44
β-strand	487-492	6	44
α-helix	498	1
β-strand	499-505	7	44
β-strand	510-517	8	44
β-strand	525-530	6	38
β-strand	533-538	6	38
β-strand	545-554	10	38

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Disintegrin and metalloproteinase domain-containing protein 22	A, B	protein	486	Homo sapiens	Q9P0K1 (AlphaFold model)
Leucine-rich glioma-inactivated protein 1	D, E	protein	526	Homo sapiens	O95970 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8HPY_1 Disintegrin and metalloproteinase domain-containing protein 22 (chains A, B)
NVEEETKYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKDQLKTRIVLVAMET
WATDNKFAISENPLITLREFMKYRRDFIKEKSDAVHLFSGSQFESSRSGAAYIGGICSLL
KGGGVNEFGKTDLMAVTLAQSLAHNIGIISDKRKLASGECKCEDTWSGCIMGDTGYYLPK
KFTQCNIEEYHDFLNSGGGACLFNKPSKLLDPPECGNGFIETGEECDCGTPAECVLEGAE
CCKKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPNIHKMDG
YSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQ
CNKRDVLCGYLLCTNIGNIPRLGELDGEITSTLVVQQGRTLNCSGGHVKLEEDVDLGYVE
DGTPCGPQMMCLEHRCLPVASFNFSTCLSSKEGTICSGNGVCSNELKCVCNRHWIGSDCN
TYFPHN

Sequence of entity 2 (D, E), FASTA

>8HPY_2 Leucine-rich glioma-inactivated protein 1 (chains D, E)
HHHHHHHKPKCPAVCTCTKDNALCENARSIPRTVPPDVISLSFVRSGFTEISEGSFLFTP
SLQLLLFTSNSFDVISDDAFIGLPHLEYLFIENNNIKSISRHTFRGLKSLIHLSLANNNL
QTLPKDIFKGLDSLTNVDLRGNSFNCDCKLKWLVEWLGHTNATVEDIYCEGPPEYKKRKI
NSLSSKDFDCIITEFAKSQDLPYQSLSIDTFSYLNDEYVVIAQPFTGKCIFLEWDHVEKT
FRNYDNITGTSTVVCKPIVIETQLYVIVAQLFGGSHIYKRDSFANKFIKIQDIEILKIRK
PNDIETFKIENNWYFVVADSSKAGFTTIYKWNGNGFYSHQSLHAWYRDTDVEYLEIVRTP
QTLRTPHLILSSSSQRPVIYQWNKATQLFTNQTDIPNMEDVYAVKHFSVKGDVYICLTRF
IGDSKVMKWGGSSFQDIQRMPSRGSMVFQPLQINNYQYAILGSDYSFTQVYNWDAEKAKF
VKFQELNVQAPRSFTHVSINKRNFLFASSFKGNTQIYKHVIVDLSA

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	12
CA	Calcium ion	Ca	8

Primary citation

Crystal structure of human LGI1-ADAM22 complex. Liu, H., Xu, F. To be published.

Other PDB entries of the same protein (UniProt Q9P0K1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7CQF 1.8 Å, Crystal structure of PSD-95 PDZ3 fused with ADAM22 C-terminal peptide
3G5C 2.36 Å, Structural and biochemical studies on the ectodomain of human ADAM22
5Y2Z 2.67 Å, Crystal structure of human LGI1 EPTP-ADAM22 complex
9KZC 2.78 Å, Cryo-EM structure of the LGI1 LRR-LGI1 EPTP-ADAM22 ECD complex
8HQ2 2.93 Å, Crystal structure of human ADAM22 in complex with human LGI1 mutant
8Y6B 3.49 Å, Structure of human LGI1-ADAM22 complex in space group P212121
9KZT 3.79 Å, Cryo-EM structure of the 3:3 LGI1-ADAM22 complex
8HQ1 4.17 Å, Crystal Structure Of Human Lgi1-Adam22 Complex In Space Group C2
5Y31 7.13 Å, Crystal structure of human LGI1-ADAM22 complex

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