1a1x

CRYSTAL STRUCTURE OF MTCP-1 INVOLVED IN T CELL MALIGNANCIES

spinqualitylabelsall models 1a1x, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1a1x is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum Disease [MTCP1_HUMAN] Note=Detected in T-cell leukemia bearing a t(X;14) translocation. Plays a key role in T-cell prolymphocytic leukemia. Function [MTCP1_HUMAN] Enhances the phosphorylation and activation of AKT1 and AKT2. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Crystal structure of MTCP-1: implications for role of TCL-1 and MTCP-1 in T cell malignancies.,Fu ZQ, Du Bois GC, Song SP, Kulikovskaya I, Virgilio L, Rothstein JL, Croce CM, Weber IT, Harrison RW Proc Natl Acad Sci U S A. 1998 Mar 31;95(7):3413-8. PMID:9520380 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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