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Volume 153, Issue 62 o& o2 i. i U0 F& P
On the cover: The complementarity determining region 3 of the heavy chain
8 H1 u$ d9 D, O(CDR H3) of vertebrate antibodies typically contains a diverse loop of <15
) E6 _! C& t2 ]1 @! X) G) v8 hamino acids and often provides a prominent role in binding antigen. Cows have & u; O4 @' g3 r Q( ^+ P
unusual CDR H3s of >60 amino acids with multiple cysteine residues. How these 1 y' k$ e% R- U1 b1 J2 j0 k
unusual antibodies form and what their structural characteristics are have not 2 A" F8 ]& w+ f) [7 r, h: m6 C
been understood. Wang et al. (pp. 1379–1393) show that these antibodies form a 1 H" {& v8 x' ~. g2 U2 J+ K
new structural domain comprised of “stalk” and “knob” features that are highly
8 m- f0 n' e7 a Idiverse in amino acid content as well as disulfide patterns. They propose that ( \% Q# H, d T, L) |* c
bovine ultralong CDR H3 antibodies create antibody diversity by somatic
; h8 _( B& A4 r# Ediversification that creates unique disulfide patterns in the knob region. The
& j$ l! m4 h- h. j. scover shows the stalk and disulfide-bonded knob of a crystal structure of a cow , Q# \7 V; g& o: d' A0 j! Y
antibody (light-green, right) overlaid onto the oil painting “Red Calf Portrait” d; p8 N6 W- w( F2 o4 h: [2 ?$ i' K
by Denise Rich.3 j/ v3 L$ V8 @* M
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