7C5D: TRF2 TRFH domain

Crystal structure of TRF2 TRFH domain in complex with a MCPH1 peptide. Determined by X-ray diffraction at 2.15 Å resolution. Released 21 Oct 2020.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,582
Mol. weight: 52.49 kDa
Released: 21 Oct 2020

Explore 7C5D in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7C5D contains 26 α-helices and 2 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: 12 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	48-69	22
α-helix	73-86	14
α-helix	94-96	3
α-helix	98-111	14
β-strand	119	1	1
α-helix	128-142	15
α-helix	147-167	21
α-helix	171-182	12
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 B: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	43-69	27
α-helix	73-86	14
α-helix	94-96	3
α-helix	98-111	14
α-helix	128-142	15
α-helix	147-167	21
α-helix	171-181	11
α-helix	189-200	12
α-helix	207-210	4
α-helix	214-226	13
α-helix	232-234	3
α-helix	235-242	8

Chain C: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	326-329	4
β-strand	336	1	1

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	326-329	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Telomeric repeat-binding factor 2	A, B	protein	204	Homo sapiens	Q15554 (AlphaFold model)
Microcephalin	C, D	protein	21	Homo sapiens	Q8NEM0 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7C5D_1 Telomeric repeat-binding factor 2 (chains A, B)
GAGEARLEEAVNRWVLKFYFHEALRAFRGSRYGDFRQIRDIMQALLVRPLGKEHTVSRLL
RVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTEAVVESSRKLVKEAA
VIICIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNIIREKNLAHPVIQNFSYETFQQKM
LRFLESHLDDAEPYLLTMAKKALK

Sequence of entity 2 (C, D), FASTA

>7C5D_2 Microcephalin (chains C, D)
SQETFEEKYRLSPTLSSTKGH

Primary citation

Microcephalin 1/BRIT1-TRF2 interaction promotes telomere replication and repair, linking telomere dysfunction to primary microcephaly. Cicconi, A., Rai, R., Xiong, X. et al. Nat Commun (2020) 11:5861-5861. DOI 10.1038/s41467-020-19674-0 · 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
3BU8 2.15 Å, Crystal Structure of TRF2 TRFH domain and TIN2 peptide complex
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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