3OSK: Human CTLA-4 apo homodimer

Crystal structure of human CTLA-4 apo homodimer. Determined by X-ray diffraction at 1.8 Å resolution. Released 8 Dec 2010.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,103
Mol. weight: 28.58 kDa
Ligands: NAG
Released: 8 Dec 2010

Explore 3OSK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3OSK contains 8 α-helices and 20 β-strands across 2 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: 5 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	5-6	2	1
β-strand	10-12	3	2
β-strand	19-25	7	1
α-helix	26-28	3
β-strand	33-42	10	2
β-strand	45-55	11	2
α-helix	59-60	2
β-strand	68-73	6	1
β-strand	76-81	6	1
α-helix	86-88	3
β-strand	90-100	11	2
α-helix	104	1
β-strand	105-108	4	2
β-strand	112-115	4	2
α-helix	119-121	3

Chain B: 3 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	5-6	2	3
β-strand	10-12	3	4
β-strand	19-25	7	3
β-strand	33-41	9	4
β-strand	46-55	10	4
β-strand	68-72	5	3
β-strand	76-81	6	3
α-helix	86-88	3
β-strand	90-100	11	4
α-helix	104	1
β-strand	105-108	4	4
β-strand	112-115	4	4
α-helix	118-121	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cytotoxic T-lymphocyte protein 4	A, B	protein	130	Homo sapiens	P16410 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3OSK_1 Cytotoxic T-lymphocyte protein 4 (chains A, B)
KAMHVAQPAVVLASSRGIASFVCEYASPGKATEVRVTVLRQADSQVTEVCAATYMMGNEL
TFLDDSICTGTSSGNQVNLTIQGLRAMDTGLYICKVELMYPPPYYLGIGNGTQIYVIDPE
PCPDSDLVPR

Ligands and cofactors

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

Water and common crystallization additives (GOL) are not listed.

Primary citation

Rigid-body ligand recognition drives cytotoxic T-lymphocyte antigen 4 (CTLA-4) receptor triggering. Yu, C., Sonnen, A.F.-P., George, R. et al. J Biol Chem (2011) 286:6685-6696. DOI 10.1074/jbc.M110.182394 · PubMed

Other PDB entries of the same protein (UniProt P16410 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7CIO 1.1 Å, Molecular interactions of cytoplasmic region of CTLA-4 with SH2 domains of PI3-kinase
9DQ3 1.64 Å, Crystal structure of engineered Ipilimumab (mipi.4) Fab in complex with human CTLA-4
5GGV 2.0 Å, CTLA-4 in complex with tremelimumab Fab
3BX7 2.1 Å, Engineered Human Lipocalin 2 (LCN2) in Complex with the Extracellular Domain of Human…
7ELX 2.14 Å, The crystal structure of CTLA-4 and Fab
7DV4 2.38 Å, Crystal structure of anti-CTLA-4 VH domain in complex with human CTLA-4
7SU0 2.41 Å, Crystal structure of an acidic pH-selective Ipilimumab variant Ipi.105 in complex with…
7SU1 2.53 Å, Crystal structure of an acidic pH-selective Ipilimumab variant Ipi.106 in complex with…
2X44 2.6 Å, Structure of a strand-swapped dimeric form of CTLA-4
6RP8 2.6 Å, Crystal Structure of Ipilimumab Fab complexed with CTLA-4 at 2.6A resolution
8GAB 2.72 Å, Crystal structure of CTLA-4 in complex with a high affinity CTLA-4 binder
1I8L 3.0 Å, Human B7-1/CTLA-4 co-stimulatory complex

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