Structural basis for SH2D1A mutations in X-linked lymphoproliferative disease

Biochem Biophys Res Commun. 2000 Mar 5;269(1):124-30. doi: 10.1006/bbrc.2000.2146.

Abstract

X-linked lymphoproliferative disease (XLP) is a rare and severe immune deficiency, characterized by abnormal immune responses to the Epstein-Barr virus. Recently, the gene responsible for XLP, SH2D1A, has been identified and shown to code for a small cytoplasmic protein with an SH2 domain that interacts with SLAM and 2B4, two receptorial molecules involved in signal transduction in T and NK cells, respectively. A variety of SH2D1A gene mutations have been reported thus far in XLP males. Here we describe a single-strand conformation polymorphism assay for mutation analysis in XLP. Four novel patients with SH2D1A mutations are described. These mutants, and the others previously reported in the literature, have been included in a Registry (SH2D1Abase) that is fully accessible on the World Wide Web. A three-dimensional model of the SH2 domain of the SH2D1A protein has been developed, based on homology with other SH2 domains. The structural consequences of disease-causing SH2D1A mutations are discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Binding Sites / genetics
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics*
  • Conserved Sequence
  • DNA Primers / genetics
  • Genetic Linkage*
  • Humans
  • Intracellular Signaling Peptides and Proteins*
  • Lymphoproliferative Disorders / genetics*
  • Male
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation*
  • Polymorphism, Single-Stranded Conformational
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Signaling Lymphocytic Activation Molecule Associated Protein
  • X Chromosome / genetics*
  • src Homology Domains / genetics

Substances

  • Carrier Proteins
  • DNA Primers
  • Intracellular Signaling Peptides and Proteins
  • SH2D1A protein, human
  • Signaling Lymphocytic Activation Molecule Associated Protein

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