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 9 v& y9 ?. S! W1 q Q' x( G
Volume 153, Issue 65 [6 }# X- A! q6 H. |0 X
On the cover: The complementarity determining region 3 of the heavy chain
: [. \" _2 H/ j. u6 |( t$ @1 a0 S, s! i(CDR H3) of vertebrate antibodies typically contains a diverse loop of <15
0 B- ~5 E& j8 M1 F k+ i9 D0 hamino acids and often provides a prominent role in binding antigen. Cows have * Y; O' R( F$ R
unusual CDR H3s of >60 amino acids with multiple cysteine residues. How these
5 | `+ k! s, C5 U) Y9 u" G' W0 Ounusual antibodies form and what their structural characteristics are have not
! C( } c Z# }% r$ c/ I# o* Ybeen understood. Wang et al. (pp. 1379–1393) show that these antibodies form a
, `: v [/ a6 W/ F0 p; cnew structural domain comprised of “stalk” and “knob” features that are highly
& e) W! t! i2 w: F8 O) e, N7 \diverse in amino acid content as well as disulfide patterns. They propose that : Q+ K V$ B4 A; P/ a
bovine ultralong CDR H3 antibodies create antibody diversity by somatic
0 }9 c# {8 k7 a4 E( U3 G2 o: l. ~diversification that creates unique disulfide patterns in the knob region. The
: o+ E+ B) W# S) J# k" Dcover shows the stalk and disulfide-bonded knob of a crystal structure of a cow * ~, I/ H+ Z1 x! L% T
antibody (light-green, right) overlaid onto the oil painting “Red Calf Portrait”
+ I! W; ?0 Y$ T7 I, ]; g8 hby Denise Rich.$ L/ Z* w9 Z; A
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发表于 2013-6-7 07:30
发表于 2013-6-7 07:57
