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Volume 153, Issue 6
8 k( o. g+ T% N* E" g2 B5 XOn the cover: The complementarity determining region 3 of the heavy chain 7 _4 G1 Y' n& U
(CDR H3) of vertebrate antibodies typically contains a diverse loop of <15
) B/ @. z9 X5 k3 Tamino acids and often provides a prominent role in binding antigen. Cows have & U( ?# e/ N [8 r* x
unusual CDR H3s of >60 amino acids with multiple cysteine residues. How these 8 X" Q+ ]4 B4 Q6 m
unusual antibodies form and what their structural characteristics are have not ) m# _0 k, Z; K+ P7 H
been understood. Wang et al. (pp. 1379–1393) show that these antibodies form a
% i s ]; h* Bnew structural domain comprised of “stalk” and “knob” features that are highly
. @5 b( q# A$ Mdiverse in amino acid content as well as disulfide patterns. They propose that
- L! l/ i, I. J# T. ebovine ultralong CDR H3 antibodies create antibody diversity by somatic
m9 `! r0 d% ?: C) Sdiversification that creates unique disulfide patterns in the knob region. The
, v% Z# `4 c, n0 Q5 ^2 R+ u8 ccover shows the stalk and disulfide-bonded knob of a crystal structure of a cow b5 T8 W A- V9 ~# e5 f! R( B/ @
antibody (light-green, right) overlaid onto the oil painting “Red Calf Portrait” 6 b6 u% G5 q1 E4 v
by Denise Rich.0 D% ]. S4 n5 c" F2 C
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发表于 2013-6-7 07:30
