{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fu ZQ"],"funding":["NCI NIH HHS"],"pagination":["3413-8"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC19850"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["95(7)"],"pubmed_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"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Crystal structure of MTCP-1: implications for role of TCL-1 and MTCP-1 in T cell malignancies."],"pmcid":["PMC19850"],"funding_grant_id":["P01 CA076259"],"pubmed_authors":["Weber IT","Song SP","Du Bois GC","Fu ZQ","Virgilio L","Rothstein JL","Croce CM","Kulikovskaya I","Harrison RW"],"additional_accession":[]},"is_claimable":false,"name":"Crystal structure of MTCP-1: implications for role of TCL-1 and MTCP-1 in T cell malignancies.","description":"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","dates":{"release":"1998-01-01T00:00:00Z","publication":"1998 Mar","modification":"2025-04-04T09:43:06.555Z","creation":"2019-03-26T22:29:06Z"},"accession":"S-EPMC19850","cross_references":{"pubmed":["9520380"],"doi":["10.1073/pnas.95.7.3413"]}}