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Characterization of the surface topography and putative tertiary structure of the human CD7 molecule.

Publication ,  Journal Article
Ware, RE; Scearce, RM; Dietz, MA; Starmer, CF; Palker, TJ; Haynes, BF
Published in: J Immunol
December 1, 1989

The CD7 gp40 molecule is a member of the Ig gene superfamily and is expressed on T cell precursors before their entry into the thymus during fetal development. N-terminal amino acids 1-107 of CD7 are highly homologous to Ig kappa-L chains whereas the carboxyl-terminal region of the extracellular domain of CD7 is proline-rich and has been postulated to form a stalk from which the Ig domain projects. To define potential functional regions of CD7, we have studied the surface topography of the CD7 Ag by synthesizing peptides corresponding to linear sequences within the CD7 extracellular domains, by raising polyclonal anti-CD7 rabbit sera against these peptides, and by computer analysis of the primary CD7 amino acid sequence. Polyclonal anti-CD7 sera were studied using indirect immunofluorescence, RIA, radioimmunoprecipitation, and Western blot assays. Computer analysis was performed comparing the CD7 sequence with all other known protein sequences. We found that three CD7 epitopes defined by peptides CD7-1A (AA 1-38), CD7-4 (AA 48-74), and CD7-7 (AA 129-146) were available for binding antibody on the surface of the CD7 molecule. Using computer analysis, we transposed the amino acid sequence of the CD7 Ig kappa-like N-terminal domain of CD7 onto the spatial coordinates of REI, a previously reported Ig kappa-molecule highly homologous (48%) to the CD7 N-terminal Ig-like region. Based on computer analysis of this putative CD7 three-dimensional structure, both the CD7-1A and CD7-4 regions protruded from the surface of the N-terminal domain of the CD7 molecule. Finally, comparison of the CD7 transmembrane sequence with CD4 and HIV transmembrane sequences and with respiratory syncytial virus fusion sequences demonstrated similar sequence motifs among these molecules.

Duke Scholars

Published In

J Immunol

ISSN

0022-1767

Publication Date

December 1, 1989

Volume

143

Issue

11

Start / End Page

3632 / 3640

Location

United States

Related Subject Headings

  • Software
  • Rabbits
  • Protein Conformation
  • Peptides
  • Peptide Mapping
  • Molecular Sequence Data
  • Membrane Glycoproteins
  • Immunology
  • Immune Sera
  • Humans
 

Citation

APA
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ICMJE
MLA
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Ware, R. E., Scearce, R. M., Dietz, M. A., Starmer, C. F., Palker, T. J., & Haynes, B. F. (1989). Characterization of the surface topography and putative tertiary structure of the human CD7 molecule. J Immunol, 143(11), 3632–3640.
Ware, R. E., R. M. Scearce, M. A. Dietz, C. F. Starmer, T. J. Palker, and B. F. Haynes. “Characterization of the surface topography and putative tertiary structure of the human CD7 molecule.J Immunol 143, no. 11 (December 1, 1989): 3632–40.
Ware RE, Scearce RM, Dietz MA, Starmer CF, Palker TJ, Haynes BF. Characterization of the surface topography and putative tertiary structure of the human CD7 molecule. J Immunol. 1989 Dec 1;143(11):3632–40.
Ware, R. E., et al. “Characterization of the surface topography and putative tertiary structure of the human CD7 molecule.J Immunol, vol. 143, no. 11, Dec. 1989, pp. 3632–40.
Ware RE, Scearce RM, Dietz MA, Starmer CF, Palker TJ, Haynes BF. Characterization of the surface topography and putative tertiary structure of the human CD7 molecule. J Immunol. 1989 Dec 1;143(11):3632–3640.

Published In

J Immunol

ISSN

0022-1767

Publication Date

December 1, 1989

Volume

143

Issue

11

Start / End Page

3632 / 3640

Location

United States

Related Subject Headings

  • Software
  • Rabbits
  • Protein Conformation
  • Peptides
  • Peptide Mapping
  • Molecular Sequence Data
  • Membrane Glycoproteins
  • Immunology
  • Immune Sera
  • Humans