《细胞》[Cell]13年6月6日出版pdf全文

nero1981

3 \! T5 s9 h+ |7 l& w' NVolume 153, Issue 6
( J$ W, B$ }( z0 m6 X  sOn the cover: The complementarity determining region 3 of the heavy chain
5 M5 p" W8 o% S2 H: Y(CDR H3) of vertebrate antibodies typically contains a diverse loop of <15
. e% M  R: s: \) X" C+ N7 O% Oamino acids and often provides a prominent role in binding antigen. Cows have
: J: [3 g% t0 b, d# L. \5 munusual CDR H3s of >60 amino acids with multiple cysteine residues. How these 2 H  [3 t/ V. w! i2 R
unusual antibodies form and what their structural characteristics are have not
5 f+ g5 f9 l% {been understood. Wang et al. (pp. 1379–1393) show that these antibodies form a
1 ]8 P# q6 W/ c* Q( D: mnew structural domain comprised of “stalk” and “knob” features that are highly . j' q) U( J; O/ P5 W' a
diverse in amino acid content as well as disulfide patterns. They propose that
% a9 E! ~: w7 f5 L; _) c, fbovine ultralong CDR H3 antibodies create antibody diversity by somatic
  t4 f! y9 y2 K3 Hdiversification that creates unique disulfide patterns in the knob region. The
" u3 D# y" v  r3 D6 Ycover shows the stalk and disulfide-bonded knob of a crystal structure of a cow : A5 j& l: c2 f
antibody (light-green, right) overlaid onto the oil painting “Red Calf Portrait” % Z3 L: T! W6 t. I+ y0 c
by Denise Rich.
$ f% t0 x/ }7 G" ^6 K

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