词条 | HMG-box |
释义 |
| Symbol = PF00505 | Name = HMG (high mobility group) box | image = 2LEF.png | width = 300px | caption = 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. | Pfam = PF00505 | InterPro = IPR009071 | SMART= | PROSITE= | SCOP = 1hsm | TCDB = | OPM family = | OPM protein = | PDB = {{PDB2|1aab}}, {{PDB2|1cg7}}, {{PDB2|1ckt}}, {{PDB2|1e7j}}, {{PDB2|1gt0}}, {{PDB2|1hme}}, {{PDB2|1hmf}}, {{PDB2|1hry}}, {{PDB2|1hrz}}, {{PDB2|1hsm}}, {{PDB2|1hsn}}, {{PDB2|1i11}}, {{PDB2|1j3x}}, {{PDB2|1j46}}, {{PDB2|1j47}}, {{PDB2|1j5n}}, {{PDB2|1k99}}, {{PDB2|1lwm}}, {{PDB2|1nhm}}, {{PDB2|1nhn}}, {{PDB2|1o4x}}, {{PDB2|1qrv}}, {{PDB2|1s9m}}, {{PDB2|1sx9}}, {{PDB2|1v64}}, {{PDB2|1wgf}}, {{PDB2|1wxl}}, {{PDB2|2crj}}, {{PDB2|2cs1}}, {{PDB2|2lef}} }} In molecular biology, the HMG-box (high mobility group box) is a protein domain which is involved in DNA binding.[1] StructureThe structure of the HMG-box domain contains three alpha helices separated by loops (see figure to the right).[2] FunctionHMG-box containing proteins only bind non-B-type DNA conformations (kinked or unwound) with high affinity.[1] HMG-box domains are found in 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] References1. ^1 {{cite journal |vauthors=Stros M, Launholt D, Grasser KD | title = The HMG-box: a versatile protein domain occurring in a wide variety of DNA-binding proteins | journal = Cell. Mol. Life Sci. | volume = 64 | issue = 19–20 | pages = 2590–606 |date=October 2007 | pmid = 17599239 | doi = 10.1007/s00018-007-7162-3 | url = }} 2. ^1 {{cite journal | author = Thomas JO | title = HMG1 and 2: architectural DNA-binding proteins | journal = Biochem. Soc. Trans. | volume = 29 | issue = Pt 4 | pages = 395–401 |date=August 2001 | pmid = 11497996 | doi = 10.1042/BST0290395}} 3. ^D. Murugesapillai et al, [https://doi.org/10.1093/nar/gku635 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, [https://link.springer.com/article/10.1007/s12551-016-0236-4 Single-molecule studies of high-mobility group B architectural DNA bending proteins], Biophys Rev (2016) doi:10.1007/s12551-016-0236-4 External links
2 : DNA-binding substances|Protein domains |
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