PDBsum entry 6o3t

Gene regulation/DNA

PDB id

6o3t

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Contents

			Protein chains

					95 a.a.


					65 a.a.

			DNA/RNA

PDB id:

6o3t

Links

Name:

Gene regulation/DNA

Title:

Structural basis of foxc2 and DNA interactions

Structure:

Forkhead box protein c2. Chain: a, b. Synonym: forkhead-related protein fkhl14,mesenchyme fork head protein 1,mfh-1 protein,transcription factor fkh-14. Engineered: yes. DNA (5'- d( Ap Ap Ap Tp Tp Gp Tp Tp Tp Ap Tp Ap Ap Ap Cp Ap Gp Cp Cp Cp G)- 3'). Chain: c.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: foxc2, fkhl14, mfh1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Synthetic construct. Organism_taxid: 32630.

Resolution:

3.06Å

R-factor:

0.235

R-free:

0.268

Authors:

H.-J.Nam,S.Li

Key ref:

S.Li et al. (2019). Crystal Structure of FOXC2 in Complex with DNA Target. ACS Omega, 4, 10906-10914. PubMed id: 31460188 DOI: 10.1021/acsomega.9b00756

Date:

27-Feb-19

Release date:

15-Jan-20

PROCHECK

	Headers

	References

Protein chain

Q99958 (FOXC2_HUMAN) - Forkhead box protein C2 from Homo sapiens

Seq: Struc:					501 a.a. 95 a.a.

Protein chain

Q99958 (FOXC2_HUMAN) - Forkhead box protein C2 from Homo sapiens

Seq: Struc:					501 a.a. 65 a.a.

Key:

PfamA domain

Secondary structure

DNA/RNA chains

		A-A-A-T-T-G-T-T-T-A-T-A-A-A-C-A-G-C-C-C-G 21 bases
		T-T-C-G-G-G-C-T-G-T-T-T-A-T-A-A-A-C-A-A-T 21 bases

DOI no: 10.1021/acsomega.9b00756	ACS Omega 4:10906-10914 (2019)
PubMed id: 31460188

Crystal Structure of FOXC2 in Complex with DNA Target.
S.Li, L.Pradhan, S.Ashur, A.Joshi, H.J.Nam.

ABSTRACT

Forkhead transcription factor C2 (FOXC2) is a transcription factor regulating vascular and lymphatic development, and its mutations are linked to lymphedema-distichiasis syndrome. FOXC2 is also a crucial regulator of the epithelial-mesenchymal transition processes essential for tumor metastasis. Here, we report the crystal structure of the FOXC2-DNA-binding domain in complex with its cognate DNA. The crystal structure provides the basis of DNA sequence recognition by FOXC2 for the T/CAAAC motif. Helix 3 makes the majority of the DNA-protein interactions and confers the DNA sequence specificity. The computational energy calculation results also validate the structural observations. The FOXC2 and DNA complex structure provides a detailed picture of protein and DNA interactions, which allows us to predict its DNA recognition specificity and impaired functions in mutants identified in human patients.