Complement Receptor Type 1 (C3b/C4b Receptor; CD35) and Complement Receptor Type 2 (C3d/Epstein-Barr Virus Receptor; CD21)

  • D. T. Fearon
  • J. M. Ahearn
Part of the Current Topics in Microbiology and Immunology book series (CT MICROBIOLOGY, volume 153)


The primary sequence of the A allotype of CR1 has been deduced from the cDNA sequence and includes a 41-residue signal peptide, an extracellular domain of 1930 residues, a 25 amino acid transmembrane domain, and a 43 amino acid cytoplasmic region (WONG et al 1985; KLICKSTEIN et al. 1987,1988; HOURCADE et al. 1988) (Fig. 1). Thirty short consensus repeats (SCRs) similar to those present in other C3/C4 binding complement proteins comprise the extracellular domain. Each SCR has four cysteines which may be disulfide bonded in the pattern, cysteine-1 to cysteine-3 and cysteine-2 to cysteine-4 (LOZIER et al. 1984; Janatova et al. 1988). These disulfide bridges create three loops of 26-29 amino acids, 12-19 amino acids, and 12-16 amino acids, respectively, in CR1. The dimensions of each SCR in CR1, 2.9 x 2.8 nm, have been estimated by electron microscopy (BARTOW et al. 1989) and are comparable to those of the SCRs of C4 binding protein (C4-bp; PERKINS et al. 1986). The regions linking SCRs are short, ranging from three to five amino acids, except for that connecting SCR-28 to SCR-29 which is seven amino acids in length. This characteristic may limit the range of motion between SCRs, perhaps accounting for the filamentous appearance of CR1.


Membrane Cofactor Protein Short Consensus Repeat Binding Complement Protein Nussenzweig Versus 
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Copyright information

© Springer-Verlag Berlin Heidelberg 1990

Authors and Affiliations

  • D. T. Fearon
    • 1
  • J. M. Ahearn
    • 1
  1. 1.Department of Medicine and The Graduate Program in ImmunologyThe Johns Hopkins University School of MedicineBaltimoreUSA

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