5NVN: Human 4EHP-4E-BP1 complex

Crystal structure of the human 4EHP-4E-BP1 complex. Determined by X-ray diffraction at 1.9 Å resolution. Released 26 Jul 2017.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,547
Mol. weight: 52.95 kDa
Released: 26 Jul 2017

Explore 5NVN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5NVN contains 17 α-helices and 19 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: 6 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	49-51	3	1
β-strand	55-65	11	2
β-strand	82-90	9	2
α-helix	91-98	8
β-strand	101	1	3
α-helix	104-106	3
β-strand	111-117	7	2
α-helix	127-129	3
β-strand	133-139	7	2
α-helix	144-156	13
β-strand	166-173	8	2
β-strand	178-184	7	2
α-helix	190-203	14
β-strand	212-216	5	2
α-helix	217-220	4

Chain B: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	56-62	7
α-helix	66-69	4
β-strand	82	1	3

Chain C: 5 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	55-66	12	1
β-strand	83-90	8	1
α-helix	91-99	9
β-strand	101	1	4
α-helix	104-106	3
β-strand	111-117	7	1
β-strand	133-139	7	1
α-helix	144-156	13
β-strand	166-173	8	1
β-strand	178-184	7	1
α-helix	190-203	14
β-strand	212-216	5	1
α-helix	218-220	3

Chain D: 4 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	56-61	6
α-helix	62-64	3
α-helix	66-69	4
α-helix	71-72	2
β-strand	82	1	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Eukaryotic translation initiation factor 4E type 2	A, C	protein	189	Homo sapiens	O60573 (AlphaFold model)
Eukaryotic translation initiation factor 4E-binding protein 1	B, D	protein	38	Homo sapiens	Q13541 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>5NVN_1 Eukaryotic translation initiation factor 4E type 2 (chains A, C)
GPHMLEAEHPLQYNYTFWYSRRTPGRPTSSQSYEQNIKQIGTFASVEQFWRFYSHMVRPG
DLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEE
ICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKMPG
RLGPQRLLF

Sequence of entity 2 (B, D), FASTA

>5NVN_2 Eukaryotic translation initiation factor 4E-binding protein 1 (chains B, D)
GPHMTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTS

Primary citation

GIGYF1/2 proteins use auxiliary sequences to selectively bind to 4EHP and repress target mRNA expression. Peter, D., Weber, R., Sandmeir, F. et al. Genes Dev (2017) 31:1147-1161. DOI 10.1101/gad.299420.117 · PubMed

Other PDB entries of the same protein (UniProt O60573 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2JGB 1.7 Å, Structure of human eIF4E homologous protein 4EHP with m7GTP
5XLN 1.9 Å, Crystal structure of the TRS_UNE-T and 4EHP complex
5NVM 2.0 Å, Crystal structure of the human 4EHP-GIGYF2 complex lacking the auxiliary sequences
5NVL 2.3 Å, Crystal structure of the human 4EHP-GIGYF2 complex
2JGC 2.4 Å, Structure of the human eIF4E homologous protein, 4EHP without ligand bound
5NVK 2.9 Å, Crystal structure of the human 4EHP-GIGYF1 complex

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