ArticleJournal of biomolecular NMR2000
Backbone dynamics and solution structure refinement of the 15N-labeled human oncogenic protein p13MTCP1: comparison with X-ray data.
Article in Journal of biomolecular NMR, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 22 citations in OpenAlex.
- Pressure and Chemical Unfolding of an α-Helical Bundle Protein: The GH2 Domain of the Protein Adaptor GIPC1.International journal of molecular sciences · 2021Article
- Systematic comparison of crystal and NMR protein structures deposited in the protein data bank.The open biochemistry journal · 2010Article
- Unraveling protein dynamics through fast spectral density mapping.Journal of biomolecular NMR · 2007Article
- Backbone dynamics of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue, by 15N NMR relaxation methods.Journal of biomolecular NMR · 2006Article
- Solution structure and backbone dynamics of the pleckstrin homology domain of the human protein kinase B (PKB/Akt). Interaction with inositol phosphates.Journal of biomolecular NMR · 2004Article
- Backbone dynamics of the cytotoxic ribonuclease alpha-sarcin by 15N NMR relaxation methods.Journal of biomolecular NMR · 2002Article
- Identification of Akt association and oligomerization domains of the Akt kinase coactivator TCL1.Molecular and cellular biology · 2002Article
- Backbone dynamics of the regulatory domain of calcium vector protein, studied by (15)N relaxation at four fields, reveals unique mobility characteristics of the intermotif linker.Protein science : a publication of the Protein Society · 2001Article
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Authors and funding
7 authors at 5 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Two related oncogenes, TCL1 and MTCP1, are overexpressed in certain T-cell prolymphocytic leukemias as a result of chromosomal rearrangements that involve the translocation of one T-cell receptor gene to either chromosome 14q32 or Xq28, respectively. The human oncoprotein p13MTCP1 is coded by the MTCP1 gene and its primary sequence is highly and only homologous to that of p14TCL1, the product of TCL1. These two proteins likely represent the first members of a new family of oncogenic proteins. A previous model of the three-dimensional solution structure of p13MTCP1 was determined recently using exclusively homonuclear proton two-dimensional NMR methods and, almost simultaneously, high-resolution crystal structures of p13MTCP1 and p14TCL1 appeared in the literature. In order to gain more insight into the details of the solution structure, we uniformly labeled p13MTCP1 with nitrogen-15. The refined structure benefits from 520 additional NOEs, extracted from either 15N-edited 3D experiments or homonuclear 2D NOESY recorded at 800 MHz, and from a nearly complete set of phi angular restraints. Measurements of 15N spin relaxation times and heteronuclear 15N[1H]NOEs at two magnetic field strengths provided additional insights into the dynamics of the protein backbone. On the basis of these new results, a putative binding surface for this particular class of oncogenes is discussed.
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