8VSB: L-tgf-b3/GARP

L-tgf-b3/GARP. Determined by electron microscopy at 2.93 Å resolution. Released 11 Sept 2024.

Method: Electron microscopy
Resolution: 2.93 Å
Organism: Homo sapiens
Chains: 3
Atoms: 7,519
Mol. weight: 155.77 kDa
Released: 11 Sept 2024

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

Secondary structure: helices and β-sheets

8VSB contains 21 α-helices and 69 β-strands across 3 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: 6 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	9-28	20
α-helix	44-55	12
β-strand	82-84	3	1
α-helix	182-189	8
β-strand	256-258	3	1
β-strand	280	1	2
α-helix	281-286	6
β-strand	293-295	3	3
β-strand	298-300	3	4
α-helix	301-305	5
β-strand	310-312	3	5
β-strand	315-317	3	4
β-strand	320-322	3	3
α-helix	353-354	2
β-strand	355-357	3	6
β-strand	360-363	4	7
β-strand	366-369	4	5
β-strand	372-375	4	5
β-strand	378-383	6	7
β-strand	385	1	2
β-strand	386-388	3	6

Chain B: 7 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	8
α-helix	10-27	18
α-helix	33-36	4
α-helix	44-51	8
β-strand	81-86	6	9
β-strand	109-110	2	10
β-strand	146-149	4	10
α-helix	186-190	5
β-strand	198-201	4	10
β-strand	254-259	6	9
β-strand	293-295	3	11
β-strand	298-300	3	12
α-helix	301-305	5
β-strand	312	1	13
β-strand	315-317	3	12
β-strand	320-322	3	11
α-helix	326-330	5
α-helix	342-345	4
β-strand	355-357	3	14
β-strand	360-369	10	13
β-strand	372-383	12	13
β-strand	386-388	3	14

Chain I: 8 helices, 39 β-strands

Element	Residues	Length	Sheet
β-strand	27-28	2	15
β-strand	32-34	3	15
β-strand	53-55	3	15
β-strand	63-64	2	16
α-helix	66-70	5
β-strand	77-79	3	15
β-strand	87-88	2	16
β-strand	101-103	3	15
α-helix	109-111	3
β-strand	128-130	3	15
β-strand	137	1	17
α-helix	141-144	4
β-strand	153-155	3	15
β-strand	160	1	17
β-strand	163-164	2	18
β-strand	177-179	3	15
β-strand	187-188	2	18
β-strand	201-203	3	15
β-strand	211-212	2	8
β-strand	222-224	3	15
β-strand	232-233	2	8
β-strand	247-249	3	15
β-strand	269-271	3	15
β-strand	319-321	3	15
α-helix	334-337	4
β-strand	343-345	3	15
β-strand	353-356	4	19
β-strand	367-369	3	15
β-strand	377-380	4	19
α-helix	381	1
β-strand	390-392	3	15
β-strand	414-416	3	15
β-strand	424	1	20
β-strand	437	1	20
β-strand	447-449	3	15
β-strand	457-458	2	21
β-strand	480-481	2	21
β-strand	495-497	3	22
α-helix	510-512	3
β-strand	518-520	3	22
β-strand	532	1	23
β-strand	540-542	3	22
β-strand	556	1	23
α-helix	559-561	3
β-strand	565-567	3	22
α-helix	579-586	8
β-strand	590	1	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transforming growth factor beta-3 proprotein	A, B	protein	389	Homo sapiens	P10600 (AlphaFold model)
Transforming growth factor beta activator LRRC32	I	protein	608	Homo sapiens	Q14392 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8VSB_1 Transforming growth factor beta-3 proprotein (chains A, B)
LSTCTTLDFGHIKKKRVEAIRGQILSKLRLTSPPEPTVMTHVPYQVLALYNSTRELLEEM
HGEREEGCTQENTESEYYAKEIHKFDMIQGLAEHNELAVCPKGITSKVFRFNVSSVEKNR
TNLFRAEFRVLRVPNPSSKRNEQRIELFQILRPDEHIAKQRYIGGKNLPTRGTAEWLSFD
VTDTVREWLLRRESNLGLEISIHCPCHTFQPNGDILENIHEVMEIKFKGVDNEDDHGRGD
LGRLKKQKDHHNPHLILMMIPPHRLDNPGQGGQRKKRALDTNYCFRNLEENCCVRPLYID
FRQDLGWKWVHEPKGYYANFCSGPCPYLRSADTTHSTVLGLYNTLNPEASASPCCVPQDL
EPLTILYYVGRTPKVEQLSNMVVKSCKCS

Sequence of entity 2 (I), FASTA

>8VSB_2 Transforming growth factor beta activator LRRC32 (chains I)
HQDKVPCKMVDKKVSCQVLGLLQVPSVLPPDTETLDLSGNQLRSILASPLGFYTALRHLD
LSTNEISFLQPGAFQALTHLEHLSLAHNRLAMATALSAGGLGPLPRVTSLDLSGNSLYSG
LLERLLGEAPSLHTLSLAENSLTRLTRHTFRDMPALEQLDLHSNVLMDIEDGAFEGLPRL
THLNLSRNSLTCISDFSLQQLRVLDLSCNSIEAFQTASQPQAEFQLTWLDLRENKLLHFP
DLAALPRLIYLNLSNNLIRLPTGPPQDSKGIHAPSEGWSALPLSAPSGNASGRPLSQLLN
LDLSYNEIELIPDSFLEHLTSLCFLNLSRNCLRTFEARRLGSLPCLMLLDLSHNALETLE
LGARALGSLRTLLLQGNALRDLPPYTFANLASLQRLNLQGNRVSPCGGPDEPGPSGCVAF
SGITSLRSLSLVDNEIELLRAGAFLHTPLTELDLSSNPGLEVATGALGGLEASLEVLALQ
GNGLMVLQVDLPCFICLKRLNLAENRLSHLPAWTQAVSLEVLDLRNNSFSLLPGSAMGGL
ETSLRRLYLQGNPLSCCGNGWLAAQLHQGRVDVDATQDLICRFSSQEEVSLSHVRPEDCE
KGGLKNIN

Primary citation

Dynamic allostery drives autocrine and paracrine TGF-beta signaling. Jin, M., Seed, R.I., Cai, G. et al. Cell (2024) 187:6200. DOI 10.1016/j.cell.2024.08.036 · PubMed

Other PDB entries of the same protein (UniProt P10600 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1TGJ 2.0 Å, Human transforming growth factor-beta 3, crystallized from dioxane
1KTZ 2.15 Å, Crystal Structure of the Human TGF-beta Type II Receptor Extracellular Domain in Complex…
4UM9 2.5 Å, Crystal structure of alpha V beta 6 with peptide
8V52 2.5 Å, Crystal structure of 2A10 Fab bound to Human TGF-beta3
8VS6 2.73 Å, L-TGF-b3/avb8
2PJY 3.0 Å, Structural basis for cooperative assembly of the TGF-beta signaling complex
9B9F 3.0 Å, Zebrafish Betaglycan Orphan Domain (zfBGo) in complex with TGF-B3 and extracellular…
3EO1 3.1 Å, Structure of the Fab Fragment of GC-1008 in Complex with Transforming Growth Factor-Beta 3
1TGK 3.3 Å, Human transforming growth factor beta 3, crystallized from peg 4000
9FK5 4.1 Å, Zebrafish Betaglycan Orphan Domain (zfBGo) in complex with TGF-B3 and extracellular…

Browse structure collections

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