Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous Abstract"Expression Profiles and Binding Properties of the Chemosensory Protein PxylCSP11 from the Diamondback Moth, Plutella xylostella (Lepidoptera: Plutellidae)"    Next AbstractChemical and physical signals mediating conspecific and heterospecific aggregation behavior of first instar stink bugs »

Proc Natl Acad Sci U S A


Title:Crystal structure of MTCP-1: implications for role of TCL-1 and MTCP-1 in T cell malignancies
Author(s):Fu ZQ; Du Bois GC; Song SP; Kulikovskaya I; Virgilio L; Rothstein JL; Croce CM; Weber IT; Harrison RW;
Address:"Kimmel Cancer Center and Department of Microbiology and Immunology, Thomas Jefferson University, 233 South 10th Street, Philadelphia, PA 19107, USA"
Journal Title:Proc Natl Acad Sci U S A
Year:1998
Volume:95
Issue:7
Page Number:3413 - 3418
DOI: 10.1073/pnas.95.7.3413
ISSN/ISBN:0027-8424 (Print) 1091-6490 (Electronic) 0027-8424 (Linking)
Abstract:"Two related oncogenes, TCL-1 and MTCP-1, are overexpressed in 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. The crystal structure of human recombinant MTCP-1 protein has been determined at 2.0 A resolution by using multiwavelength anomalous dispersion data from selenomethionine-enriched protein and refined to an R factor of 0.21. MTCP-1 folds into a compact eight-stranded beta barrel structure with a short helix between the fourth and fifth strands. The topology is unique. The structure of TCL-1 has been predicted by molecular modeling based on 40% amino acid sequence identity with MTCP-1. The identical residues are clustered inside the barrel and on the surface at one side of the barrel. The overall structure of MTCP-1 superficially resembles the structures of proteins in the lipocalin family and calycin superfamily. These proteins have diverse functions, including transport of retinol, fatty acids, chromophores, pheromones, synthesis of prostaglandin, immune modulation, and cell regulation. However, MTCP-1 differs in the topology of the beta strands. The structural similarity suggests that MTCP-1 and TCL-1 form a unique family of beta barrel proteins that is predicted to bind small hydrophobic ligands and function in cell regulation"
Keywords:"Amino Acid Sequence Crystallography, X-Ray Humans Leukemia, T-Cell/*metabolism Models, Molecular Molecular Sequence Data *Protein Folding Proto-Oncogene Proteins/chemistry/metabolism Recombinant Proteins/chemistry/metabolism Sequence Analysis;"
Notes:"MedlineFu, Z Q Du Bois, G C Song, S P Kulikovskaya, I Virgilio, L Rothstein, J L Croce, C M Weber, I T Harrison, R W eng P01 CA076259/CA/NCI NIH HHS/ Research Support, Non-U.S. Gov't 1998/05/09 Proc Natl Acad Sci U S A. 1998 Mar 31; 95(7):3413-8. doi: 10.1073/pnas.95.7.3413"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 25-11-2024