HMG-box

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1aab, 1cg7, 1ckt, 1e7j, 1gt0, 1hme, 1hmf, 1hry, 1hrz, 1hsm, 1hsn, 1i11, 1j3x, 1j46, 1j47, 1j5n, 1k99, 1lwm, 1nhm, 1nhn, 1o4x, 1qrv, 1s9m, 1sx9, 1v64, 1wgf, 1wxl, 2crj, 2cs1, 2lef

HMG (high mobility group) box
HMG (high mobility group) box
	NMR structure of the HMG-box domain of the LEF1 protein (rainbow colored, N-terminus = blue, C-terminus = red) complexed with DNA (brown) based on the PDB: 2LEF coordinates.
Identifiers
Symbol	PF00505
Pfam	PF00505
InterPro	IPR009071
SCOP2	1hsm / SCOPe / SUPFAM
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1aab, 1cg7, 1ckt, 1e7j, 1gt0, 1hme, 1hmf, 1hry, 1hrz, 1hsm, 1hsn, 1i11, 1j3x, 1j46, 1j47, 1j5n, 1k99, 1lwm, 1nhm, 1nhn, 1o4x, 1qrv, 1s9m, 1sx9, 1v64, 1wgf, 1wxl, 2crj, 2cs1, 2lef

In molecular biology, the HMG-box (high mobility group box) is a protein domain which is involved in DNA binding.^[1]

Structure[]

The structure of the HMG-box domain contains three alpha helices separated by loops (see figure to the right).^[2]

Function[]

HMG-box containing proteins only bind non-B-type DNA conformations (kinked or unwound) with high affinity.^[1] HMG-box domains are found in some high mobility group proteins, which are involved in the regulation of DNA-dependent processes such as transcription, replication, and DNA repair, all of which require changing the conformation of chromatin.^[2] The single and the double box HMG proteins alter DNA architecture by inducing bends upon binding.^[3]^[4]

References[]

^ ^a ^b Stros M, Launholt D, Grasser KD (October 2007). "The HMG-box: a versatile protein domain occurring in a wide variety of DNA-binding proteins". Cell. Mol. Life Sci. 64 (19–20): 2590–606. doi:10.1007/s00018-007-7162-3. PMID 17599239. S2CID 28156847.
^ ^a ^b Thomas JO (August 2001). "HMG1 and 2: architectural DNA-binding proteins". Biochem. Soc. Trans. 29 (Pt 4): 395–401. doi:10.1042/BST0290395. PMID 11497996.
^ D. Murugesapillai et al, DNA bridging and looping by HMO1 provides a mechanism for stabilizing nucleosome-free chromatin, Nucleic Acids Res (2014) 42 (14): 8996-9004
^ D. Murugesapillai et al, Single-molecule studies of high-mobility group B architectural DNA bending proteins, Biophys Rev (2016) doi:10.1007/s12551-016-0236-4

External links[]

HMG-Box Domains at the US National Library of Medicine Medical Subject Headings (MeSH)

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[pmid17599239-1] Stros M, Launholt D, Grasser KD (October 2007). "The HMG-box: a versatile protein domain occurring in a wide variety of DNA-binding proteins". Cell. Mol. Life Sci. 64 (19–20): 2590–606. doi:10.1007/s00018-007-7162-3. PMID 17599239. S2CID 28156847.

[pmid11497996-2] Thomas JO (August 2001). "HMG1 and 2: architectural DNA-binding proteins". Biochem. Soc. Trans. 29 (Pt 4): 395–401. doi:10.1042/BST0290395. PMID 11497996.

[3] D. Murugesapillai et al, DNA bridging and looping by HMO1 provides a mechanism for stabilizing nucleosome-free chromatin, Nucleic Acids Res (2014) 42 (14): 8996-9004

[4] D. Murugesapillai et al, Single-molecule studies of high-mobility group B architectural DNA bending proteins, Biophys Rev (2016) doi:10.1007/s12551-016-0236-4

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