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