title: Structural evaluation and analyses of tumor differentiation factor.
abstract: Tumor differentiation factor (TDF) is a protein produced by the pituitary and secreted into the blood stream. The mechanism of its action has still not been elucidated, although the associated protein receptor was identified. Furthermore, the TDF protein does not have any homology with other known proteins, and the crystal structure of TDF also is not available at this time. To gain some insight into the structure of this rather underexplored protein, we have performed a molecular dynamics simulation of a model TDF structure. The structural stability of this protein is evaluated as a function of time. The time dependent structural changes of four cysteine residues present in this structure also are explored.
authors.affiliation: Structural Biology Unit, Biochemistry and Proteomics Group, Department of Chemistry and Biomolecular Science, Clarkson University, 8 Clarkson Avenue, Potsdam, NY, 13699-5810, USA.
authors.forename: Urmi
authors.initials: U
authors.lastname: Roy
authors.forename: Alisa G
authors.initials: AG
authors.lastname: Woods
authors.forename: Izabela
authors.initials: I
authors.lastname: Sokolowska
authors.forename: Costel C
authors.initials: CC
authors.lastname: Darie
mesh_terms: D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D056004:Molecular Dynamics Simulation; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D009419:Nerve Tissue Proteins; C483315:PDF protein, human; D011994:Recombinant Proteins
references.citation: Gene. 2012 Oct 25;508(2):188-96
references.pmid: 22824468
references.citation: J Mol Psychiatry. 2013 Jun 05;1(1):8
references.pmid: 25408901
references.citation: J Am Chem Soc. 2007 May 30;129(21):6726-35
references.pmid: 17487969
references.citation: J Comput Chem. 2004 Oct;25(13):1605-12
references.pmid: 15264254
references.citation: Biochemistry. 2013 Jan 29;52(4):569-87
references.pmid: 23298176
references.citation: Nat Protoc. 2010 Apr;5(4):725-38
references.pmid: 20360767
references.citation: BMC Bioinformatics. 2008 Jan 23;9:40
references.pmid: 18215316
references.citation: Biochemistry. 1982 May 11;21(10):2259-74
references.pmid: 6178423
references.citation: J Bacteriol. 2011 Dec;193(23):6517-28
references.pmid: 21965559
references.citation: Cell Mol Life Sci. 2013 Aug;70(16):2835-48
references.pmid: 23076253
references.citation: Proc Natl Acad Sci U S A. 2005 May 10;102(19):6679-85
references.pmid: 15870208
references.citation: Proteins. 2008 Mar;70(4):1235-42
references.pmid: 17853448
references.citation: Proc Natl Acad Sci U S A. 2004 Feb 10;101(6):1560-5
references.pmid: 14745005
references.citation: Curr Med Chem. 2012;19(36):6081-94
references.pmid: 23150945
references.citation: Comput Biol Chem. 2012 Aug;39:29-34
references.pmid: 22885776
references.citation: J Mol Graph. 1996 Feb;14(1):33-8, 27-8
references.pmid: 8744570
references.citation: FEBS J. 2012 Jul;279(14):2579-94
references.pmid: 22613557
references.citation: J Biol Chem. 2012 Jan 13;287(3):1719-33
references.pmid: 22130669
references.citation: J Mol Graph Model. 2011 Aug;29(8):1015-24
references.pmid: 21605994
references.citation: Endocrinology. 1992 Dec;131(6):2573-80
references.pmid: 1446601
references.citation: Biotechnol Appl Biochem. 2012 Nov-Dec;59(6):445-50
references.pmid: 23586953
references.citation: Arch Biochem Biophys. 2013 Mar;531(1-2):128-35
references.pmid: 23266569
references.citation: Biochem Res Int. 2010;2010:213936
references.pmid: 21188070
references.citation: Cell Mol Life Sci. 2006 Jan;63(2):207-19
references.pmid: 16389462