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Volume 153, Issue 6
' w8 G8 [$ @6 W2 g; h' UOn the cover: The complementarity determining region 3 of the heavy chain
; o& o1 Z( Z8 a8 p1 a, T(CDR H3) of vertebrate antibodies typically contains a diverse loop of <15
( Y2 C$ |5 O1 Z( x' C) _* K4 r7 Uamino acids and often provides a prominent role in binding antigen. Cows have
/ | b, x/ s7 y: q3 j/ q, l- Cunusual CDR H3s of >60 amino acids with multiple cysteine residues. How these % Z3 h, m/ T3 l9 ]% r9 n7 |
unusual antibodies form and what their structural characteristics are have not # O8 m& R0 K# U/ j6 M- }0 q/ H* p
been understood. Wang et al. (pp. 1379–1393) show that these antibodies form a # B% N' ^! L. C$ \
new structural domain comprised of “stalk” and “knob” features that are highly
3 ]$ v# Z: v/ s1 b! ?diverse in amino acid content as well as disulfide patterns. They propose that ; \, g4 ^0 b: n5 \$ ?+ K
bovine ultralong CDR H3 antibodies create antibody diversity by somatic 5 h" _$ q3 S1 a+ J; a @8 f
diversification that creates unique disulfide patterns in the knob region. The 4 y1 J6 |+ o" T
cover shows the stalk and disulfide-bonded knob of a crystal structure of a cow 5 @5 v- d; J# O) o, S( T
antibody (light-green, right) overlaid onto the oil painting “Red Calf Portrait”
* I6 E7 i% c1 L" `by Denise Rich./ U+ o" l' k, F0 p+ b! v
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