6GFF: GARP

Structure of GARP (LRRC32) in complex with latent TGF-beta1 and MHG-8 Fab. Determined by X-ray diffraction at 3.1 Å resolution. Released 7 Nov 2018.

Method: X-ray diffraction
Resolution: 3.1 Å
Organisms: Homo sapiens, Mus musculus
Chains: 14
Atoms: 21,668
Mol. weight: 398.36 kDa
Released: 7 Nov 2018

Explore 6GFF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6GFF contains 107 α-helices and 218 β-strands across 14 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: 9 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	31-32	2	1
α-helix	38-56	19
α-helix	62-64	3
α-helix	69	1
α-helix	73-74	2
α-helix	75-85	11
α-helix	99-102	4
β-strand	106-111	6	2
β-strand	132-134	3	3
α-helix	137-143	7
α-helix	147-149	3
β-strand	150-159	10	2
β-strand	166-171	6	3
β-strand	183-187	5	3
β-strand	194-199	6	2
α-helix	201-208	8
β-strand	216-221	6	3
β-strand	257-262	6	2

Chain B: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	280-281	2	4
α-helix	282-285	4
β-strand	294-296	3	5
α-helix	297	1
β-strand	299-301	3	6
β-strand	311-313	3	4
β-strand	316-318	3	6
β-strand	321-323	3	5
α-helix	337-345	9
β-strand	356-370	15	4
β-strand	373-389	17	4

Chain C: 13 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	38-56	19
α-helix	62-64	3
α-helix	68-69	2
α-helix	73-74	2
α-helix	75-85	11
α-helix	100-102	3
β-strand	106-112	7	4
α-helix	113-115	3
α-helix	120-123	4
β-strand	131-136	6	7
α-helix	137-143	7
α-helix	147-149	3
β-strand	150-159	10	4
β-strand	162	1	8
β-strand	166-173	8	7
β-strand	179-187	9	7
β-strand	190	1	8
β-strand	194-199	6	4
α-helix	201-209	9
β-strand	214-221	8	7
β-strand	257-262	6	4
α-helix	265-267	3
α-helix	272-273	2

Chain D: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	282-285	4
β-strand	294-296	3	9
α-helix	297	1
β-strand	300-301	2	10
β-strand	311-313	3	2
β-strand	316-317	2	10
β-strand	321-323	3	9
α-helix	337-340	4
α-helix	341-346	6
β-strand	356-370	15	2
β-strand	373-389	17	2

Chain E: 12 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	31-32	2	11
α-helix	38-56	19
α-helix	62-64	3
α-helix	68-69	2
α-helix	73-74	2
α-helix	75-85	11
α-helix	98-102	5
β-strand	106-112	7	12
α-helix	113-115	3
α-helix	120-123	4
β-strand	130-136	7	13
α-helix	137-143	7
α-helix	147-149	3
β-strand	150-159	10	12
β-strand	162	1	14
β-strand	166-173	8	13
β-strand	179-187	9	13
β-strand	190	1	14
β-strand	194-199	6	12
α-helix	201-209	9
β-strand	214-221	8	13
β-strand	224	1	15
β-strand	227	1	15
β-strand	236	1	12
β-strand	257-262	6	12
α-helix	265-267	3

Chain F: 2 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	280-281	2	16
α-helix	282-285	4
β-strand	294-296	3	17
β-strand	299-301	3	18
β-strand	311-313	3	16
β-strand	316-318	3	18
β-strand	321-323	3	17
α-helix	339-345	7
β-strand	356-370	15	16
β-strand	373-389	17	16

Chain G: 14 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	38-56	19
α-helix	62-64	3
α-helix	68-69	2
α-helix	73-74	2
α-helix	75-85	11
α-helix	100-102	3
β-strand	106-112	7	16
α-helix	113-115	3
α-helix	116-120	5
α-helix	121-123	3
β-strand	130-136	7	19
α-helix	137-143	7
α-helix	147-149	3
β-strand	150-159	10	16
β-strand	162	1	20
β-strand	166-172	7	19
β-strand	180-187	8	19
β-strand	190	1	20
β-strand	194-199	6	16
α-helix	201-209	9
β-strand	214-221	8	19
α-helix	230-232	3
β-strand	236	1	16
β-strand	257-262	6	16
α-helix	265-267	3

Chain H: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	294-296	3	21
α-helix	297	1
β-strand	299-301	3	22
β-strand	311-313	3	12
β-strand	316-318	3	22
β-strand	321-323	3	21
α-helix	327-329	3
α-helix	337-340	4
α-helix	341-346	6
β-strand	356-370	15	12
β-strand	373-389	17	12

6 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, C, E, G	protein	249	Homo sapiens	P01137 (AlphaFold model)
Transforming growth factor beta-1	B, D, F, H	protein	112	Homo sapiens	P01137 (AlphaFold model)
Leucine-rich repeat-containing protein 32	I, J	protein	618	Homo sapiens	Q14392 (AlphaFold model)
MHG-8 Fab light chain	K, M	protein	212	Mus musculus
MHG-8 Fab heavy chain	L, N	protein	221	Mus musculus

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

>6GFF_1 Transforming growth factor beta-1 (chains A, C, E, G)
LSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVA
GESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVL
LSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLS
RGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQ
HLQSSRHRR

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

>6GFF_2 Transforming growth factor beta-1 (chains B, D, F, H)
ALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSK
VLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS

Sequence of entity 3 (I, J), FASTA

>6GFF_3 Leucine-rich repeat-containing protein 32 (chains I, J)
HQDKVPCKMVDKKVSCQVLGLLQVPSVLPPDTETLDLSGNQLRSILASPLGFYTALRHLD
LSTNEISFLQPGAFQALTHLEHLSLAHNRLAMATALSAGGLGPLPRVTSLDLSGNSLYSG
LLERLLGEAPSLHTLSLAENSLTRLTRHTFRDMPALEQLDLHSNVLMDIEDGAFEGLPRL
THLNLSRNSLTCISDFSLQQLRVLDLSCNSIEAFQTASQPQAEFQLTWLDLRENKLLHFP
DLAALPRLIYLNLSNNLIRLPTGPPQDSKGIHAPSEGWSALPLSAPSGNASGRPLSQLLN
LDLSYNEIELIPDSFLEHLTSLCFLNLSRNCLRTFEARRLGSLPCLMLLDLSHNALETLE
LGARALGSLRTLLLQGNALRDLPPYTFANLASLQRLNLQGNRVSPCGGPDEPGPSGCVAF
SGITSLRSLSLVDNEIELLRAGAFLHTPLTELDLSSNPGLEVATGALGGLEASLEVLALQ
GNGLMVLQVDLPCFICLKRLNLAENRLSHLPAWTQAVSLEVLDLRNNSFSLLPGSAMGGL
ETSLRRLYLQGNPLSCCGNGWLAAQLHQGRVDVDATQDLICRFSSQEEVSLSHVRPEDCE
KGGLKNINLEAAENLYFQ

Sequence of entity 4 (K, M), FASTA

>6GFF_4 MHG-8 Fab light chain (chains K, M)
DIQVTQSSSYLSVSLGDRVTITCKASDHIKNWLAWYQQKPGIAPRLLVSGATSLEAGVPS
RFSGSGSGKNFTLSITSLQTEDVATYYCQQYWSTPWTFGGGTTLEIRRADAAPTVSIFPP
SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLT
LTKDEYERHNSYTCEATHKTSTSPIVKSFNRN

Sequence of entity 5 (L, N), FASTA

>6GFF_5 MHG-8 Fab heavy chain (chains L, N)
QVQLKESGPGLVAPSQSLSITCTVSGFSLTGYGINWVRQPPGKGLEWLGMIWSDGSTDYN
SVLTSRLRISKDNSNSQVFLKMNSLQVDDTARYYCARDRNYYDYDGAMDYWGQGTSVTVS
SAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQS
DLYTLSSSVTVPSSTWPSQTVTCNVAHPASSTKVDKKIVPR

Primary citation

Structural basis of latent TGF-beta 1 presentation and activation by GARP on human regulatory T cells. Lienart, S., Merceron, R., Vanderaa, C. et al. Science (2018) 362:952-956. DOI 10.1126/science.aau2909 · 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
8REW 2.98 Å, CryoEM structure of human GARP-lTGFbeta1 in complex with a Fab fragment derived from an…
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…
8VSD 3.2 Å, avb8/L-TGF-b1/GARP

Browse structure collections

About this viewer

MolViewer shows 6GFF directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.