3BU8: TRF2 TRFH domain and TIN2 peptide complex

Crystal Structure of TRF2 TRFH domain and TIN2 peptide complex. Determined by X-ray diffraction at 2.15 Å resolution. Released 19 Feb 2008.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,760
Mol. weight: 58.27 kDa
Released: 19 Feb 2008

Explore 3BU8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3BU8 contains 22 α-helices and 2 β-strands across 3 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: 11 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	48-69	22
α-helix	73-86	14
α-helix	95-111	17
β-strand	118-119	2	1
α-helix	128-142	15
α-helix	147-167	21
α-helix	171-181	11
α-helix	186-188	3
α-helix	189-201	13
α-helix	207-210	4
α-helix	214-226	13
α-helix	235-243	9

Chain B: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	44-69	26
α-helix	73-86	14
α-helix	95-111	17
α-helix	128-142	15
α-helix	147-167	21
α-helix	171-181	11
α-helix	189-201	13
α-helix	207-210	4
α-helix	214-226	13
α-helix	232-234	3
α-helix	235-243	9

Chain C: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	264-265	2	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Telomeric repeat-binding factor 2	A, B	protein	235	Homo sapiens	Q15554 (AlphaFold model)
TERF1-interacting nuclear factor 2	C, D	protein	19	Homo sapiens	Q9BSI4 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3BU8_1 Telomeric repeat-binding factor 2 (chains A, B)
GAGEARLEEAVNRWVLKFYFHEALRAFRGSRYGDFRQIRDIMQALLVRPLGKEHTVSRLL
RVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTEAVVESSRKLVKEAA
VIICIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNIIREKNLAHPVIQNFSYETFQQKM
LRFLESHLDDAEPYLLTMAKKALKSESAASSTGKEDKQPAPGPVEKPPREPARQL

Sequence of entity 2 (C, D), FASTA

>3BU8_2 TERF1-interacting nuclear factor 2 (chains C, D)
SFNLAPLGRRRVQSQWAST

Primary citation

A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins. Chen, Y., Yang, Y., van Overbeek, M. et al. Science (2008) 319:1092-1096. DOI 10.1126/science.1151804 · PubMed

Other PDB entries of the same protein (UniProt Q15554 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3SJM 1.35 Å, Crystal Structure Analysis of TRF2-Dbd-DNA complex
1W0U 1.8 Å, hTRF2 DNA-binding domain in complex with telomeric DNA.
3K6G 1.95 Å, Crystal structure of Rap1 and TRF2 complex
4M7C 2.05 Å, Crystal structure of the TRF2-binding motif of SLX4 in complex with the TRFH domain of…
6J67 2.05 Å, Crystal structure of the compound 34 in a complex with TRF2
7C5D 2.15 Å, Crystal structure of TRF2 TRFH domain in complex with a MCPH1 peptide
1H6P 2.2 Å, Dimeristion domain from human TRF2
5XYF 2.2 Å, Crystal structure of the human TIN2-TPP1-TRF2 telomeric complex
4RQI 2.44 Å, Structure of TRF2/RAP1 secondary interaction binding site
3BUA 2.5 Å, Crystal Structure of TRF2 TRFH domain and APOLLO peptide complex
9Q9K 2.59 Å, Cryo-EM structure of human Mre11-Rad50 (MR) complex bound to DNA and telomeric factor…
9Q9J 2.71 Å, Cryo-EM structure of human Mre11-Rad50-Nbs1 (MRN) complex bound to DNA and telomeric…

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