2Q86: Mouse invariant NKT cell receptor Valpha14

Structure of the mouse invariant NKT cell receptor Valpha14. Determined by X-ray diffraction at 1.85 Å resolution. Released 1 Apr 2008.

Method: X-ray diffraction
Resolution: 1.85 Å
Organism: Mus musculus
Chains: 4
Atoms: 7,258
Mol. weight: 108.79 kDa
Ligands: NAG
Released: 1 Apr 2008

Explore 2Q86 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2Q86 contains 23 α-helices and 83 β-strands across 4 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: 4 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	1
β-strand	9-13	5	2
β-strand	18-24	7	1
β-strand	32-37	6	2
β-strand	43-49	7	2
β-strand	53-58	6	1
β-strand	61-66	6	1
β-strand	71-76	6	1
α-helix	81-83	3
β-strand	85-91	7	2
α-helix	94-96	3
β-strand	98-99	2	2
β-strand	103-108	6	2
β-strand	117-122	6	3
β-strand	130-137	8	3
α-helix	141-146	6
β-strand	151-153	3	3
β-strand	157-160	4	3
β-strand	167-175	9	3
α-helix	182-185	4

Chain B: 7 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	4
β-strand	10-14	5	5
β-strand	19-25	7	4
β-strand	31-38	8	5
β-strand	42-49	8	5
β-strand	56-57	2	5
β-strand	65-67	3	4
β-strand	73-78	6	4
α-helix	83-85	3
β-strand	87-95	9	5
β-strand	98-101	4	5
β-strand	105-110	6	5
α-helix	113-115	3
β-strand	117	1	6
α-helix	118-119	2
β-strand	120-124	5	7
β-strand	125	1	3
α-helix	126-127	2
α-helix	128-134	7
β-strand	136-146	11	7
β-strand	147	1	6
β-strand	151-157	7	8
β-strand	160-162	3	8
β-strand	166-168	3	7
β-strand	173-176	4	7
β-strand	179-189	11	7
α-helix	190-193	4
β-strand	199-206	8	8
β-strand	209	1	9
α-helix	220-221	2
β-strand	223	1	9
β-strand	225-232	8	8

Chain C: 5 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	10
β-strand	9-13	5	2
β-strand	18-24	7	10
β-strand	31-37	7	2
β-strand	43-49	7	2
β-strand	53-58	6	10
β-strand	61-66	6	10
β-strand	71-76	6	10
α-helix	81-83	3
β-strand	85-92	8	2
β-strand	97-99	3	2
α-helix	100	1
β-strand	103-108	6	2
β-strand	117-122	6	11
β-strand	130-137	8	11
α-helix	141-144	4
β-strand	152-153	2	11
α-helix	154-156	3
β-strand	157-160	4	11
β-strand	167-174	8	11
α-helix	182-185	4
β-strand	190	1	11

Chain D: 7 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	12
β-strand	10-14	5	13
β-strand	19-25	7	12
β-strand	31-38	8	13
β-strand	42-49	8	13
β-strand	56-57	2	13
β-strand	65-67	3	12
β-strand	73-78	6	12
α-helix	83-85	3
β-strand	87-95	9	13
β-strand	98-101	4	13
β-strand	105-110	6	13
α-helix	113-115	3
β-strand	117	1	14
α-helix	118-119	2
β-strand	120-124	5	15
β-strand	125	1	11
α-helix	126-127	2
α-helix	128-134	7
β-strand	136-146	11	15
β-strand	147	1	14
β-strand	151-157	7	16
β-strand	160-162	3	16
β-strand	166-168	3	15
α-helix	172	1
β-strand	173-176	4	15
β-strand	179-189	11	15
α-helix	190-193	4
β-strand	199-206	8	16
β-strand	209	1	17
β-strand	223	1	17
β-strand	225-232	8	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Valpha14 TCR	A, C	protein	229	Mus musculus	P01849 (AlphaFold model)
Vbeta8.2	B, D	protein	254	Mus musculus	P01851 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>2Q86_1 Valpha14 TCR (chains A, C)
KTQVEQSPQSLVVRQGENCVLQCNYSVTPDNHLRWYKQDTGKGLVLLTVLVDQKDKTSNG
RYSATLDKDAKHSTLHITATLLDDTATYFCVVGDRGSALFGSGTQLIVIPYIQNPEPAVY
QLKDPRSQDSTLCLFTDFDSQINVPKTMESGTFITDKCVLDMKAMDSKSNGAIAWSNQTS
FTCQDIFKETNATYPSSDVPCDATLTEKSFETDMNLNFQNLSSADLVPR

Sequence of entity 2 (B, D), FASTA

>2Q86_2 Vbeta8.2 (chains B, D)
EAAVTQSPRNKVAVTGGKVTLSCNQTNNHNNMYWYRQDTGHGLRLIHYSYGAGSTEKGDI
PDGYKASRPSQENFSLILELATPSQTSVYFCASGGGGTLYFGAGTRLSVLEDLRNVTPPK
VSLFEPSKAEIANKQKATLVCLARGFFPDHVELSWWVNGKEVHSGVCTDPQAYKESNYSY
CLSSRLRVSATFWHNPRNHFRCQVQFHGLSEEDKWPEGSPKPVTQNISAEAWGRADCGIT
SASYHQSSADLVPR

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1

Primary citation

Crystal Structures of Mouse CD1d-iGb3 Complex and its Cognate Valpha14 T Cell Receptor Suggest a Model for Dual Recognition of Foreign and Self Glycolipids. Zajonc, D.M., Savage, P.B., Bendelac, A. et al. J Mol Biol (2008) 377:1104-1116. DOI 10.1016/j.jmb.2008.01.061 · PubMed

Other PDB entries of the same protein (UniProt P01849 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5M02 1.75 Å, Crystal structure of murine P14 TCR / H-2Db with PF, modified gp33 peptide from LCMV
6G9Q 1.89 Å, Ternary complex of P14 TCR with murine MHC class I H-2 Db in complex with self-antigen…
5M01 1.95 Å, Crystal structure of murine P14 TCR/ H-2Db complex with PA, modified gp33 peptide from…
1LP9 2.0 Å, Xenoreactive complex AHIII 12.2 TCR bound to p1049/HLA-A2.1
8WTE 2.17 Å, Crystal structure of TCR in complex with HLA-A*11:01 bound to KRAS-G12V peptide…
8WUL 2.36 Å, Crystal structure of affinity enhanced TCR in complex with HLA-A*11:01 bound to…
2JCC 2.5 Å, AH3 recognition of mutant HLA-A2 W167A
1NFD 2.8 Å, An alpha-beta T cell receptor (TCR) heterodimer in complex with an anti-TCR FAB fragment…
2J8U 2.88 Å, Large CDR3a loop alteration as a function of MHC mutation.
3MBE 2.89 Å, TCR 21.30 in complex with MHC class II I-Ag7HEL(11-27)
3C6L 3.4 Å, Crystal structure of mouse MHC class II I-Ab/3K peptide complexed with mouse TCR 2W20
6MF8 TCR alpha transmembrane domain

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