Crystals of the Msx-1 homeodomain-DNA complex have been obtained by hanging-drop vapor diffusion at 293 K in 12% PEG 4000 and 0.1 M sodium acetate pH 4.6. The homeodomain consists of 60 amino acids and is the DNA-binding domain. The DNA in the complex was 16 base pairs with the sequence 5'-TGTCACTAATTGAAGG-3', containing an overhang T at each end. The crystals diffract to 2.15 A (99.8% completeness) using cryogenic (123 K) conditions. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 33.66, b = 60.96, c = 83.37 A. The structure will illuminate the details of Msx-1-DNA binding specificity and clarify its role in transcriptional regulation. Mutations in Msx-1 cause craniofacial deformities in mice.
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http://dx.doi.org/10.1107/s0907444999012081 | DOI Listing |
J Biomol Struct Dyn
May 2016
a Bioinformatics Centre , CSIR-Institute of Microbial Technology, Sector 39A, Chandigarh , India.
In most of homeodomain-DNA complexes, glutamine or lysine is present at 50th position and interacts with 5th and 6th nucleotide of core recognition region. Molecular dynamics simulations of Msx-1-DNA complex (Q50-TG) and its variant complexes, that is specific (Q50K-CC), nonspecific (Q50-CC) having mutation in DNA and (Q50K-TG) in protein, have been carried out. Analysis of protein-DNA interactions and structure of DNA in specific and nonspecific complexes show that amino acid residues use sequence-dependent shape of DNA to interact.
View Article and Find Full Text PDFBiochemistry
October 2001
Michigan State University Chemistry Department, East Lansing Michigan 48824, USA.
The Msx-1 homeodomain protein plays a crucial role in craniofacial, limb, and nervous system development. Homeodomain DNA-binding domains are comprised of 60 amino acids that show a high degree of evolutionary conservation. We have determined the structure of the Msx-1 homeodomain complexed to DNA at 2.
View Article and Find Full Text PDFActa Crystallogr D Biol Crystallogr
December 1999
Michigan State University Chemistry Department, East Lansing, MI 48824, USA.
Crystals of the Msx-1 homeodomain-DNA complex have been obtained by hanging-drop vapor diffusion at 293 K in 12% PEG 4000 and 0.1 M sodium acetate pH 4.6.
View Article and Find Full Text PDFMol Cell Biol
February 1995
Center for Advanced Biotechnology and Medicine, UMDNJ-Robert Wood Johnson Medical School, Piscataway.
This study investigates the transcriptional properties of Msx-1, a murine homeodomain protein which has been proposed to play a key role in regulating the differentiation and/or proliferation state of specific cell populations during embryogenesis. We show, using basal and activated transcription templates, that Msx-1 is a potent repressor of transcription and can function through both TATA-containing and TATA-less promoters. Moreover, repression in vivo and in vitro occurs in the absence of DNA-binding sites for the Msx-1 homeodomain.
View Article and Find Full Text PDFMol Endocrinol
November 1994
Department of Bone Biology and Osteoporosis Research, Merck/Merck Research Laboratories, West Point, Pennsylvania 19486.
We recently defined an element (ACTAATTGG) within the rat osteocalcin (OC) promoter at -84 to -92 which provides approximately 70% of basal promoter activity in osteoblastic cell lines and binds a specific nuclear factor found in OC-producing ROS 17/2.8 osteosarcoma cells. Since this element closely resembles the recently described Msx-1 (Hox 7.
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