2PJY: Transforming growth factor beta-3

Structural basis for cooperative assembly of the TGF-beta signaling complex. Determined by X-ray diffraction at 3.0 Å resolution. Released 5 Feb 2008.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 3
Atoms: 2,337
Mol. weight: 33.69 kDa
Released: 5 Feb 2008

Explore 2PJY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2PJY contains 7 α-helices and 27 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: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	1
α-helix	4-7	4
β-strand	16-18	3	2
β-strand	21-23	3	3
α-helix	24-28	5
β-strand	33-35	3	4
β-strand	38-40	3	3
β-strand	43-45	3	2
β-strand	54	1	1
α-helix	57-68	12
β-strand	78-80	3	1
β-strand	83-92	10	4
β-strand	95-106	12	4
β-strand	108-111	4	1

Chain B: 2 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	21	1	5
α-helix	22-26	5
β-strand	27-29	3	4
β-strand	32-35	4	6
β-strand	43-45	3	7
β-strand	51-53	3	4
β-strand	60-67	8	6
β-strand	72-79	8	6
β-strand	98-99	2	7
β-strand	101-105	5	6
β-strand	108-115	8	6
α-helix	120-122	3
β-strand	123-125	3	7

Chain C: 2 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	10-13	4	8
β-strand	23-26	4	8
β-strand	29-35	7	5
β-strand	42-48	7	5
α-helix	60-62	3
α-helix	65-68	4
β-strand	72-77	6	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transforming growth factor beta-3	A	protein	112	Homo sapiens	P10600 (AlphaFold model)
TGF-beta receptor type-2	B	protein	108	Homo sapiens	P37173 (AlphaFold model)
TGF-beta receptor type-1	C	protein	79	Homo sapiens	P36897 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2PJY_1 Transforming growth factor beta-3 (chains A)
ALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKGYYANFCSGPCPYLRSADTTHST
VLGLYNTLNPEASASPCCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS

Sequence of entity 2 (B), FASTA

>2PJY_2 TGF-beta receptor type-2 (chains B)
AGAVKFPQLCKFCDVRFSTCDNQKSCMSNCSITSICEKPQEVCVAVWRKNDENITLETVC
HDPKLPYHDFILEDAASPKCIMKEKKKPGETFFMCSCSSDECNDNIIF

Sequence of entity 3 (C), FASTA

>2PJY_3 TGF-beta receptor type-1 (chains C)
ALQCFCHLCTKDNFTCVTDGLCFVSVTETTDKVIHNSSCIAEIDLIPRDRPFVCAPSSKT
GSVTTTYCCNQDHCNKIEL

Primary citation

Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding. Groppe, J., Hinck, C.S., Samavarchi-Tehrani, P. et al. Mol Cell (2008) 29:157-168. DOI 10.1016/j.molcel.2007.11.039 · 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
8VSB 2.93 Å, L-tgf-b3/GARP
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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