Blue Baroque

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Blue Baroque
A performance-art piece by David Mason,
interpreted by G. Prody. Friday May 10, 8 pm,
Bellingham Unitarian Fellowship.
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Seminar Today for POINTS!!! 315 pm, SL 140
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Immunology Antibodies
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The three-dimensional structure of an
antigen- antibody complex as determined by x-ray
diffraction analysis . The protein antigen,
which is the enzyme lysozyme, is shown in green
. The antigen-binding site of the Fab fragment
of the antibody is formed by both the light chain
( yellow ) and the heavy chain ( blue ).About 20
amino acid residues in the binding site contact
a similar number of residues on the lysozyme
surface. In (B) the antigen and antibody have
been pulled apart to reveal their complementary
contacting surfaces. The bit of the antigen that
protrudes from the complementary surface (shown
in red ) is a glutamine residue. In (C) the
separated molecules have been rotated about 90
degrees around the vertical axis from (A) to
show the interacting surfaces the amino acid
side chains that interact are shown in red, with
the protruding glutamine now in pink . In
several other antibody molecules that have been
studied in this way, the antigen-binding site
(for a small antigenic determinant) isformed by
a much deeper cleft. (From A. Amit, R. Mariuzza,
S. Phillips, and R. Poljak, S cience
233747-753, 1986.)
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Ig Heavy MW Effector
functions class chain IgM
? 900,000 B-cell receptor Activates
complement IgG ? 150,000 Crosses
placenta Binds to Fc receptors of
phagocytes Activates complement IgA
? 150,000-600,000 Mucosal transport IgE
? 190,000 Induces mast cell degranulation IgD ?
150,000 B-cell receptor
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From Hozumi and Tonegawa, 1976, PNAS USA 73 3628
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VVP Fig. 27-39
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Models for recombination of Ig genes V and J. A.
Deletional joining occurs when the gene segments
have the same transcriptional orientation (blue
arrows). B. Inversional joining occurs when the
gene segments have opposite transcriptional
orientations.
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Class switching
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The T-Cell Receptor

• Variations on a Theme by Molecules of the Ig
  Superfamily!

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Fig. 9.1 Self-MHC restriction of the TCR.
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Overview of TCR Recombination
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Test of the dual-receptor and altered-self
models. Data supports the altered-self model. Al
tered-self model One receptor can recognize
foreign antigen AND self MHC. Dual receptor
Two T-cell receptors, one for self MHC, the
other for Ag.
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Structural similarities between Ig and TCR.
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Production and Identification of cDNAs coding
the TCR by subtractive hybridization.
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Germ-line organization of murine TCR genes.
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Gene Rearrangements
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Affinity constants and Roles of Co-receptors in
TCR binding.
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TCR-MHC-peptide structures.
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TCR-MHC-peptide structures --top view with TCR a
(red) and ß (yellow) variable regions.
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TCR viewed from above showing surfaces involved
in binding the MHC-peptide complex. HV4
hypervariable domain 4 of the beta subunit.
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HIV buds out of cells.
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VVP Fig. 27-42 Heme controlled protein synthesis
in reticulocytes.