8REW: Human GARP-lTGFbeta1

CryoEM structure of human GARP-lTGFbeta1 in complex with a Fab fragment derived from an activating antibody. Determined by electron microscopy at 2.98 Å resolution. Released 26 Mar 2025.

Method: Electron microscopy
Resolution: 2.98 Å
Organisms: Homo sapiens, Lama glama
Chains: 9
Atoms: 12,428
Mol. weight: 356.57 kDa
Ligands: NAG
Released: 26 Mar 2025

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

Secondary structure: helices and β-sheets

8REW contains 36 α-helices and 121 β-strands across 9 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: 8 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	31	1	1
α-helix	38-56	19
α-helix	62-64	3
α-helix	72-74	3
α-helix	75-85	11
β-strand	106-112	7	2
α-helix	113-115	3
α-helix	119-122	4
β-strand	130-134	5	3
α-helix	137-143	7
β-strand	150-159	10	2
β-strand	162	1	4
β-strand	166-173	8	3
β-strand	179-187	9	3
β-strand	190	1	4
β-strand	194-199	6	2
α-helix	201-209	9
β-strand	216-221	6	3
β-strand	235	1	2
β-strand	257-262	6	2

Chain B: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	282-287	6
β-strand	294-296	3	5
β-strand	299-301	3	6
α-helix	302-306	5
β-strand	311-313	3	7
β-strand	316-318	3	6
β-strand	321-323	3	5
α-helix	329-331	3
α-helix	341-345	5
β-strand	356-370	15	7
β-strand	373-389	17	7

Chain C: 8 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	38-56	19
α-helix	62-64	3
α-helix	75-85	11
β-strand	106-112	7	7
α-helix	113-115	3
α-helix	120-123	4
β-strand	130-136	7	8
α-helix	137-143	7
α-helix	147-149	3
β-strand	150-159	10	7
β-strand	162	1	9
β-strand	166-173	8	8
β-strand	179-187	9	8
β-strand	190	1	9
β-strand	194-199	6	7
α-helix	201-210	10
β-strand	214-221	8	8
β-strand	235	1	7
β-strand	257-262	6	7

Chain D: 1 helix, 7 β-strands

Element	Residues	Length	Sheet
β-strand	294-296	3	10
β-strand	299-301	3	11
β-strand	311-313	3	2
β-strand	316-318	3	11
β-strand	321-323	3	10
α-helix	340-344	5
β-strand	356-370	15	2
β-strand	373-389	17	2

Chain E: 8 helices, 36 β-strands

Element	Residues	Length	Sheet
β-strand	32-34	3	12
β-strand	53-55	3	12
β-strand	63-64	2	13
α-helix	66-69	4
β-strand	77-79	3	12
β-strand	87-88	2	13
β-strand	100-103	4	12
β-strand	128-130	3	12
β-strand	137	1	14
α-helix	141-144	4
β-strand	153-155	3	12
β-strand	160	1	14
β-strand	163-164	2	15
β-strand	177-179	3	12
β-strand	187-188	2	15
β-strand	201-203	3	12
β-strand	212	1	16
β-strand	214	1	1
β-strand	222-224	3	12
β-strand	233	1	16
β-strand	247-249	3	12
β-strand	269-271	3	12
β-strand	319-321	3	12
β-strand	329	1	17
α-helix	332-336	5
β-strand	343-345	3	12
β-strand	353-356	4	17
β-strand	367-369	3	12
β-strand	377-380	4	17
α-helix	381	1
β-strand	390-392	3	12
β-strand	414-416	3	12
α-helix	422-425	4
β-strand	447-449	3	12
β-strand	457	1	18
β-strand	470-472	3	12
β-strand	480	1	18
α-helix	481-482	2
β-strand	495-497	3	12
β-strand	518-520	3	12
β-strand	540-542	3	12
α-helix	553-556	4
β-strand	565-566	2	12
α-helix	580-585	6

Chain F: 2 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	23-25	3	19
β-strand	28-31	4	20
β-strand	36-43	8	19
β-strand	55-59	5	20
β-strand	66-70	5	20
β-strand	74-75	2	20
α-helix	76	1
β-strand	83-88	6	19
β-strand	91-97	7	19
α-helix	101-103	3
β-strand	105-113	9	20
β-strand	120-123	4	20
β-strand	127-131	5	20

Chain G: 1 helix, 12 β-strands

Element	Residues	Length	Sheet
β-strand	22-26	5	21
β-strand	29-31	3	22
β-strand	35-44	10	21
α-helix	48-50	3
β-strand	53-58	6	22
β-strand	64-70	7	22
β-strand	77-79	3	22
β-strand	84	1	21
β-strand	87-92	6	21
β-strand	97-105	9	21
β-strand	111-118	8	22
β-strand	127-130	4	22
β-strand	134-138	5	22

Chain H: 2 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	22-26	5	23
β-strand	30-31	2	24
β-strand	36-44	9	23
α-helix	48-50	3
β-strand	53-58	6	25
β-strand	64-70	7	25
β-strand	77-79	3	25
β-strand	84	1	23
β-strand	87-92	6	23
β-strand	97-103	7	23
α-helix	107-109	3
β-strand	111-117	7	25
β-strand	130	1	25
β-strand	134-136	3	25
β-strand	137-138	2	24

1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transforming growth factor beta-1	A, B, C, D	protein	390	Homo sapiens	P01137 (AlphaFold model)
Transforming growth factor beta activator LRRC32	E	protein	674	Homo sapiens	Q14392 (AlphaFold model)
hFab LHT-22, Light Chain	F, I	protein	238	Lama glama
hFab LHT-22, Heavy Chain	G, H	protein	247	Lama glama

Sequence of entity 1 (A, B, C, D), FASTA

>8REW_1 Transforming growth factor beta-1 (chains A, B, C, D)
MPPSGLRLLPLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLA
SPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEI
YDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWR
YLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFT
TGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYI
DFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQA
LEPLPIVYYVGRKPKVEQLSNMIVRSCKCS

Sequence of entity 2 (E), FASTA

>8REW_2 Transforming growth factor beta activator LRRC32 (chains E)
MRPQILLLLALLTLGLAAQHQDKVPCKMVDKKVSCQVLGLLQVPSVLPPDTETLDLSGNQ
LRSILASPLGFYTALRHLDLSTNEISFLQPGAFQALTHLEHLSLAHNRLAMATALSAGGL
GPLPRVTSLDLSGNSLYSGLLERLLGEAPSLHTLSLAENSLTRLTRHTFRDMPALEQLDL
HSNVLMDIEDGAFEGLPRLTHLNLSRNSLTCISDFSLQQLRVLDLSCNSIEAFQTASQPQ
AEFQLTWLDLRENKLLHFPDLAALPRLIYLNLSNNLIRLPTGPPQDSKGIHAPSEGWSAL
PLSAPSGNASGRPLSQLLNLDLSYNEIELIPDSFLEHLTSLCFLNLSRNCLRTFEARRLG
SLPCLMLLDLSHNALETLELGARALGSLRTLLLQGNALRDLPPYTFANLASLQRLNLQGN
RVSPCGGPDEPGPSGCVAFSGITSLRSLSLVDNEIELLRAGAFLHTPLTELDLSSNPGLE
VATGALGGLEASLEVLALQGNGLMVLQVDLPCFICLKRLNLAENRLSHLPAWTQAVSLEV
LDLRNNSFSLLPGSAMGGLETSLRRLYLQGNPLSCCGNGWLAAQLHQGRVDVDATQDLIC
RFSSQEEVSLSHVRPEDCEKGGLKNINLEAAAENLYFQGAAWSHPQFEKGAAWSHPQFEK
GAAWSHPQFEKGAA

Sequence of entity 3 (F, I), FASTA

>8REW_3 hFab LHT-22, Light Chain (chains F, I)
MGWSCIILFLVATATGVHSQAVVTQEPSLSVSPGGTVTITCGLSSGSVTRNNYPDWYQQT
PGQAPRLLLYNTVARHSGVPSRFSGSISGNKAALTITGAQPEDEAGYYCALYMYTGSNNG
RVFGGGTLLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSP
VKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS

Sequence of entity 4 (G, H), FASTA

>8REW_4 hFab LHT-22, Heavy Chain (chains G, H)
MGWSCIILFLVATATGVHSELQLVESGGGLVQPGGSLRLSCAASGFTFDDYTMNWVRQAP
GKGLEWVSAIRWNGVTTYYAESMKGRFTVSRDNGQNTLYLQMNSLKAEDTAVYYCAKGGS
IDLTYGMDYWGKGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVS
WNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEP
KSCDKTH

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	5

Primary citation

Antibody-mediated TGF-beta 1 activation for the treatment of diseases caused by deleterious T cell activity. Lambert, F., Felix, J., Wautier, S. et al. Cell Rep (2025) 44:116061-116061. DOI 10.1016/j.celrep.2025.116061 · PubMed

Other PDB entries of the same protein (UniProt P01137 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8UDZ 2.21 Å, The Structure of LTBP-49247 Fab Bound to TGFbeta1 Small Latent Complex
9VJJ 2.48 Å, Crystal Structure of human Latent TGF-beta1 in complex with SOF10
8C7H 2.7 Å, Cryo-EM Map of the latTGF-beta LHG-10 Fab complex
13FJ 2.75 Å, TGFB1 in complex with NIS793 FAB
6OM2 2.77 Å, Crystal structure of atypical integrin alphaV beta8 with proTGF-beta1 ligand peptide
5VQP 2.9 Å, Crystal structure of human pro-TGF-beta1
3KFD 3.0 Å, Ternary complex of TGF-b1 reveals isoform-specific ligand recognition and receptor…
4KV5 3.0 Å, scFv GC1009 in complex with TGF-beta1.
8VSC 3.0 Å, L-tgf-b1/GARP
9R3S 3.06 Å, pro-TGF-beta1 in complex with the third TB Domain from Latent Transforming Growth…
6GFF 3.1 Å, Structure of GARP (LRRC32) in complex with latent TGF-beta1 and MHG-8 Fab
8VSD 3.2 Å, avb8/L-TGF-b1/GARP

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