4MNQ: PDB entry 4MNQ

TCR-peptide specificity overrides affinity enhancing TCR-MHC interactions. Determined by X-ray diffraction at 2.74 Å resolution. Released 13 Nov 2013.

Method: X-ray diffraction
Resolution: 2.74 Å
Organisms: Homo sapiens, Pan troglodytes
Chains: 5
Atoms: 6,684
Mol. weight: 94.57 kDa
Released: 13 Nov 2013

Explore 4MNQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4MNQ contains 23 α-helices and 75 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: 10 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-12	10	1
α-helix	20	1
β-strand	21-28	8	1
β-strand	31-37	7	1
β-strand	46-47	2	1
α-helix	50-54	5
α-helix	57-84	28
β-strand	94-103	10	1
β-strand	109-118	10	1
β-strand	121-126	6	1
β-strand	133-135	3	1
α-helix	138-149	12
α-helix	152-157	6
α-helix	158-163	6
α-helix	164-173	10
α-helix	176-179	4
β-strand	183	1	2
α-helix	184-186	3
β-strand	187-193	7	3
β-strand	198-208	11	3
β-strand	209	1	2
β-strand	214-219	6	4
β-strand	222-224	3	4
β-strand	228-230	3	3
β-strand	234-235	2	3
β-strand	241-250	10	3
α-helix	254-256	3
β-strand	257-262	6	4
β-strand	270-273	4	4

Chain B: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	5
α-helix	4-5	2
β-strand	6-11	6	6
β-strand	21-30	10	6
β-strand	31	1	5
β-strand	36-41	6	7
β-strand	45	1	7
β-strand	50-51	2	6
α-helix	52-54	3
β-strand	55-56	2	6
β-strand	62-70	9	6
β-strand	78-83	6	7
α-helix	90	1
β-strand	91-94	4	7

Chain D: 4 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	5-6	2	8
β-strand	12-13	2	9
β-strand	19-24	6	8
β-strand	28-36	9	10
β-strand	42-48	7	10
β-strand	54-56	3	8
β-strand	60-65	6	8
β-strand	69-74	6	8
α-helix	79-81	3
β-strand	83-91	9	10
β-strand	100-101	2	10
β-strand	105-107	3	10
β-strand	109-110	2	9
α-helix	111-112	2
β-strand	119-124	6	11
β-strand	125	1	12
β-strand	132-137	6	11
α-helix	146-148	3
β-strand	153-155	3	11
α-helix	156-158	3
β-strand	159-163	5	11
β-strand	168-177	10	11
β-strand	198	1	11

Chain E: 6 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	13
β-strand	10-14	5	14
β-strand	20-21	2	15
β-strand	22-25	4	13
β-strand	31-37	7	14
β-strand	43-49	7	14
β-strand	56-57	2	14
β-strand	64-65	2	15
β-strand	73	1	13
β-strand	76-78	3	15
α-helix	83-85	3
β-strand	87-94	8	14
β-strand	100-102	3	14
β-strand	106-111	6	14
β-strand	118	1	16
β-strand	121-125	5	12
α-helix	126-128	3
α-helix	129-135	7
β-strand	137-147	11	12
β-strand	148	1	16
β-strand	152-158	7	17
β-strand	162	1	17
β-strand	167-169	3	12
α-helix	173	1
β-strand	174-175	2	12
α-helix	183-184	2
β-strand	185-194	10	12
α-helix	195-198	4
β-strand	204-211	8	17
β-strand	214	1	18
β-strand	228	1	18
β-strand	230-237	8	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
HLA class I histocompatibility antigen, A-2 alpha chain	A	protein	276	Homo sapiens	P04439 (AlphaFold model)
Beta-2-microglobulin	B	protein	100	Homo sapiens	P61769 (AlphaFold model)
Telomerase reverse transcriptase	C	protein	9	Homo sapiens	O14746 (AlphaFold model)
Uncharacterized protein, T-cell receptor, sp3.4 alpha chain	D	protein	200	Pan troglodytes, Homo sapiens	H2RG00 (AlphaFold model), K7N5N2
V_segment translation product, T-cell receptor beta-1 chain C region	E	protein	240	Homo sapiens	P01850

Sequence of entity 1 (A), FASTA

>4MNQ_1 HLA class I histocompatibility antigen, A-2 alpha chain (chains A)
GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYW
DGETRKVKAHSQTHRVDLGTLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG
KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETLQ
RTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT
FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP

Sequence of entity 2 (B), FASTA

>4MNQ_2 Beta-2-microglobulin (chains B)
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

Sequence of entity 3 (C), FASTA

>4MNQ_3 Telomerase reverse transcriptase (chains C)
ILAKFLHWL

Sequence of entity 4 (D), FASTA

>4MNQ_4 Uncharacterized protein, T-cell receptor, sp3.4 alpha chain (chains D)
IQVEQSPPDLILQEGANSTLRCNFSDSVNNLWWFHQNPWGQLINLFYIPSGTKQNGRLSA
TTVATERYSLLYISSSQTTDSGVYFCAVDSATALPYGYIFGTGTRLKVLANIQNPDPAVY
QLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWSNKSD
FACANAFNNSIIPEDTFFPS

Sequence of entity 5 (E), FASTA

>4MNQ_5 V_segment translation product, T-cell receptor beta-1 chain C region (chains E)
AGVTQTPKFQVLKTGQSMTLQCAQDMNHEYMSWYRQDPGMGLRLIHYSIHPEYTDQGEVP
NGYNVSRSTTEDFPLRLLSAAPSQTSVYFCASSYQGTEAFFGQGTRLTVVEDLNKVFPPE
VAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQPALN
DSRYALSSRLRVSATFWQDPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRAD

Primary citation

T-cell receptor (TCR)-peptide specificity overrides affinity-enhancing TCR-major histocompatibility complex interactions. Cole, D.K., Miles, K.M., Madura, F. et al. J Biol Chem (2014) 289:628-638. DOI 10.1074/jbc.M113.522110 · PubMed

Other PDB entries of the same protein (UniProt P04439 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3MRE 1.1 Å, Crystal Structure of MHC class I HLA-A2 molecule complexed with EBV bmlf1-280-288…
3D25 1.3 Å, Crystal structure of HA-1 minor histocompatibility antigen bound to human class I MHC…
3MRG 1.3 Å, Crystal Structure of MHC class I HLA-A2 molecule complexed with HCV NS3-1073-1081…
6JOZ 1.35 Å, Crystal structure of BRLF peptide from EBV in complex with HLA-A1101.
5C0G 1.37 Å, HLA-A02 carrying YLGGPDFPTI
5N1Y 1.39 Å, HLA-A02 carrying MVWGPDPLYV
1I4F 1.4 Å, Crystal structure of HLA-A*0201/MAGE-A4-peptide complex
1OGA 1.4 Å, A structural basis for immunodominant human T-cell receptor recognition.
3MRB 1.4 Å, Crystal Structure of MHC class I HLA-A2 molecule complexed with HCMV pp65-495-503…
3MRK 1.4 Å, Crystal Structure of MHC class I HLA-A2 molecule complexed with AFP137 nonapeptide
6J2A 1.4 Å, The structure of HLA-A*3003/NP44
1X7Q 1.45 Å, Crystal structure of HLA-A*1101 with sars nucleocapsid peptide

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