Solution Structure of the Human HSPC280 Protein

Overview

Journal Protein Sci

Specialty Biochemistry

Date 2010 Nov 18

PMID 21082705

Citations 6

Authors

Jinzhong Lin

Tao Zhou

Jinfeng Wang

Affiliations

Soon will be listed here.

Abstract

The human HSPC280 protein belongs to a new family of low molecular weight proteins, which is only present in eukaryotes, and is absent in fungi. The solution structure of HSPC280 was determined using multidimensional NMR spectroscopy. The overall structure consists of three α-helices and four antiparallel β-strands and has a winged helix-like fold. However, HEPC280 is not a typical DNA-binding winged helix protein in that it lacks DNA-binding activity. Unlike most winged-helix proteins, HSPC280 has an unusually long 13-residue (P62-V74) wing 1 loop connecting the β3 and β4 strands of the protein. Molecules of HSPC280 have a positively charged surface on one side and a negatively charged surface on the other side of the protein structure. Comparisons with the C-terminal 80-residue domain of proteins in the Abra family reveal a conserved hydrophobic groove in the HSPC280 family, which may allow HSPC280 to interact with other proteins.

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References

Weigelt J, Climent I, Dahlman-Wright K, Wikstrom M . Solution structure of the DNA binding domain of the human forkhead transcription factor AFX (FOXO4). Biochemistry. 2001; 40(20):5861-9. DOI: 10.1021/bi001663w. View

Jin C, Marsden I, Chen X, Liao X . Dynamic DNA contacts observed in the NMR structure of winged helix protein-DNA complex. J Mol Biol. 1999; 289(4):683-90. DOI: 10.1006/jmbi.1999.2819. View

Moseley H, Monleon D, Montelione G . Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data. Methods Enzymol. 2001; 339:91-108. DOI: 10.1016/s0076-6879(01)39311-4. View

Caffarel M, Moreno-Bueno G, Cerutti C, Palacios J, Guzman M, Mechta-Grigoriou F . JunD is involved in the antiproliferative effect of Delta9-tetrahydrocannabinol on human breast cancer cells. Oncogene. 2008; 27(37):5033-44. DOI: 10.1038/onc.2008.145. View

Overdier D, Porcella A, Costa R . The DNA-binding specificity of the hepatocyte nuclear factor 3/forkhead domain is influenced by amino-acid residues adjacent to the recognition helix. Mol Cell Biol. 1994; 14(4):2755-66. PMC: 358641. DOI: 10.1128/mcb.14.4.2755-2766.1994. View

Hong M, Fuangthong M, Helmann J, Brennan R . Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family. Mol Cell. 2005; 20(1):131-41. DOI: 10.1016/j.molcel.2005.09.013. View

Yan W, Lee H, Yi E, Reiss D, Shannon P, Kwieciszewski B . System-based proteomic analysis of the interferon response in human liver cells. Genome Biol. 2004; 5(8):R54. PMC: 507879. DOI: 10.1186/gb-2004-5-8-r54. View

Wasinger V, Locke V, Raftery M, Larance M, Rothemund D, Liew A . Two-dimensional liquid chromatography/tandem mass spectrometry analysis of Gradiflow fractionated native human plasma. Proteomics. 2005; 5(13):3397-401. DOI: 10.1002/pmic.200401160. View

Schwieters C, Kuszewski J, Tjandra N, Clore G . The Xplor-NIH NMR molecular structure determination package. J Magn Reson. 2003; 160(1):65-73. DOI: 10.1016/s1090-7807(02)00014-9. View

10.

Holm L, Rosenstrom P . Dali server: conservation mapping in 3D. Nucleic Acids Res. 2010; 38(Web Server issue):W545-9. PMC: 2896194. DOI: 10.1093/nar/gkq366. View

11.

Greening D, Glenister K, Kapp E, Moritz R, Sparrow R, Lynch G . Comparison of human platelet membrane-cytoskeletal proteins with the plasma proteome: Towards understanding the platelet-plasma nexus. Proteomics Clin Appl. 2010; 2(1):63-77. DOI: 10.1002/prca.200780067. View

12.

Troidl K, Ruding I, Cai W, Mucke Y, Grossekettler L, Piotrowska I . Actin-binding rho activating protein (Abra) is essential for fluid shear stress-induced arteriogenesis. Arterioscler Thromb Vasc Biol. 2009; 29(12):2093-101. DOI: 10.1161/ATVBAHA.109.195305. View

13.

Gajiwala K, Chen H, Cornille F, Roques B, Reith W, MACH B . Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding. Nature. 2000; 403(6772):916-21. DOI: 10.1038/35002634. View

14.

Wang I, Stepaniants S, Boie Y, Mortimer J, Kennedy B, Elliott M . Gene expression profiling in patients with chronic obstructive pulmonary disease and lung cancer. Am J Respir Crit Care Med. 2007; 177(4):402-11. DOI: 10.1164/rccm.200703-390OC. View

15.

Shiyanova T, Liao X . The dissociation rate of a winged helix protein-DNA complex is influenced by non-DNA contact residues. Arch Biochem Biophys. 1999; 362(2):356-62. DOI: 10.1006/abbi.1998.1040. View

16.

Cornilescu G, Delaglio F, Bax A . Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR. 1999; 13(3):289-302. DOI: 10.1023/a:1008392405740. View

17.

Molina H, Bunkenborg J, Reddy G, Muthusamy B, Scheel P, Pandey A . A proteomic analysis of human hemodialysis fluid. Mol Cell Proteomics. 2005; 4(5):637-50. DOI: 10.1074/mcp.M500042-MCP200. View

18.

Van Dongen M, Cederberg A, Carlsson P, Enerback S, Wikstrom M . Solution structure and dynamics of the DNA-binding domain of the adipocyte-transcription factor FREAC-11. J Mol Biol. 2000; 296(2):351-9. DOI: 10.1006/jmbi.1999.3476. View

19.

van der Heul-Nieuwenhuijsen L, Hendriksen P, van der Kwast T, Jenster G . Gene expression profiling of the human prostate zones. BJU Int. 2006; 98(4):886-97. DOI: 10.1111/j.1464-410X.2006.06427.x. View

20.

Zheng N, FRAENKEL E, Pabo C, Pavletich N . Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP. Genes Dev. 1999; 13(6):666-74. PMC: 316551. DOI: 10.1101/gad.13.6.666. View