8CN1: HDLG1-PDZ1

hDLG1-PDZ1 in complex with a TAX1 peptide from HTLV-1. Determined by X-ray diffraction at 2.09 Å resolution. Released 2 Aug 2023.

Method: X-ray diffraction
Resolution: 2.09 Å
Organisms: Homo sapiens, Human T-cell leukemia virus type I
Chains: 24
Atoms: 9,661
Mol. weight: 156.87 kDa
Released: 2 Aug 2023

Explore 8CN1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8CN1 contains 35 α-helices and 130 β-strands across 24 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: 2 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	221-228	8	5
β-strand	230	1	6
β-strand	233	1	6
β-strand	236-240	5	5
β-strand	253-258	6	5
β-strand	259	1	7
α-helix	263-267	5
β-strand	275-279	5	5
β-strand	282-283	2	5
α-helix	289-297	9
β-strand	302-309	8	5

Chain B: 4 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	18-26	9	1
α-helix	27	1
β-strand	28	1	2
β-strand	31	1	2
β-strand	34-38	5	1
β-strand	45	1	3
β-strand	48	1	3
β-strand	51-56	6	1
β-strand	57	1	4
α-helix	61-65	5
α-helix	72	1
β-strand	73-77	5	1
β-strand	80-81	2	1
α-helix	87-95	9
β-strand	100-108	9	1

Chain C: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	220-228	9	8
α-helix	229	1
β-strand	230	1	9
β-strand	233	1	9
β-strand	236-240	5	8
β-strand	253-258	6	8
α-helix	263-267	5
α-helix	274	1
β-strand	275-279	5	8
β-strand	282-283	2	8
α-helix	289-297	9
β-strand	302-310	9	8

Chains D and J: 2 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	220-228	9	10
β-strand	230	1	11
β-strand	233	1	11
β-strand	236-240	5	10
β-strand	247	1	12
β-strand	250	1	12
β-strand	253-258	6	10
α-helix	263-267	5
β-strand	275-279	5	10
β-strand	282-283	2	10
α-helix	289-297	9
β-strand	302-310	9	10

Chain E: 2 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	221-228	8	13
β-strand	230	1	14
β-strand	233	1	14
β-strand	236-240	5	13
β-strand	247	1	15
β-strand	250	1	15
β-strand	253-258	6	13
α-helix	263-267	5
β-strand	275-279	5	13
β-strand	282-283	2	13
α-helix	289-297	9
β-strand	302-309	8	13

Chain F: 2 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	220-228	9	16
β-strand	230	1	17
β-strand	233	1	17
β-strand	236-240	5	16
β-strand	253-258	6	16
α-helix	263-267	5
β-strand	275-279	5	16
β-strand	282-283	2	16
α-helix	289-297	9
β-strand	302-310	9	16

Chain G: 5 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	215	1	18
β-strand	219-228	10	19
α-helix	229	1
β-strand	230	1	20
β-strand	233	1	20
β-strand	236-239	4	19
β-strand	247	1	21
β-strand	250	1	21
β-strand	253-258	6	19
β-strand	259	1	22
α-helix	263-267	5
α-helix	274	1
β-strand	275-279	5	19
β-strand	282-283	2	19
α-helix	289-297	9
β-strand	302-311	10	19
α-helix	312	1

Chain H: 4 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	220-228	9	23
β-strand	230	1	24
β-strand	233	1	24
β-strand	236-240	5	23
β-strand	247	1	25
β-strand	250	1	25
β-strand	253-258	6	23
α-helix	263-267	5
α-helix	274	1
β-strand	275-279	5	23
β-strand	282-283	2	23
α-helix	289-297	9
β-strand	302-310	9	23
α-helix	311-312	2

10 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Disks large homolog 1	A, B, C, D, E, F, G, H, I, J, K, L	protein	116	Homo sapiens	Q12959 (AlphaFold model)
Glu-thr-glu-val	N, O, P, Q, R, T, U, V, W, X, Y, Z	protein	4	Human T-cell leukemia virus type I	P03409

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L), FASTA

>8CN1_1 Disks large homolog 1 (chains A, B, C, D, E, F, G, H, I, J, K, L)
GPLGSETPTYVNGTDADYEYEEITLERGNSGLGFSIAGGTDNPHIGDDSSIFITKIITGG
AAAQDGRLRVNDCILRVNEVDVRDVTHSKAVEALKEAGSIVRLYVKRRKPVSEKIM

Sequence of entity 2 (N, O, P, Q, R, T, U, V, W, X, Y, Z), FASTA

>8CN1_2 GLU-THR-GLU-VAL (chains N, O, P, Q, R, T, U, V, W, X, Y, Z)
ETEV

Primary citation

Identification of small molecule antivirals against HTLV-1 by targeting the hDLG1-Tax-1 protein-protein interaction. Maseko, S.B., Brammerloo, Y., Van Molle, I. et al. Antiviral Res (2023) 217:105675-105675. DOI 10.1016/j.antiviral.2023.105675 · PubMed

Other PDB entries of the same protein (UniProt Q12959 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7PC3 1.95 Å, The second PDZ domain of DLG1 complexed with the PDZ-binding motif of HTLV1-TAX1
2X7Z 2.0 Å, Crystal Structure of the SAP97 PDZ2 I342W C378A mutant protein domain
4G69 2.0 Å, Structure of the Human Discs Large 1 PDZ2 - Adenomatous Polyposis Coli Cytoskeletal…
3RL8 2.2 Å, Crystal structure of hDLG1-PDZ2 complexed with APC
3W9Y 2.2 Å, Crystal structure of the human DLG1 guanylate kinase domain
3RL7 2.3 Å, Crystal structure of hDLG1-PDZ1 complexed with APC
4AMH 2.3 Å, Influence of circular permutation on the folding pathway of a PDZ domain
8CN3 2.71 Å, hDLG1-PDZ2 in complex with a TAX1 peptide from HTLV-1
1PDR 2.8 Å, Crystal structure of the third PDZ domain from the human homolog of discs large protein
3LRA 2.95 Å, Structural Basis for Assembling a Human Tripartite Complex Dlg1-MPP7-Mals3
2M3M Solution structure of a complex consisting of hDlg/SAP-97 residues 318-406 and HPV51…
2OQS Structure of the hDLG/SAP97 PDZ2 in complex with HPV-18 papillomavirus E6 peptide

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