《细胞》[Cell]13年6月6日出版pdf全文

nero1981

+ c* @: K# \2 B6 ^; X& L. r
Volume 153, Issue 6
* M  v% _9 _3 e& VOn the cover: The complementarity determining region 3 of the heavy chain 5 m4 @; z6 W, {& o/ R+ E1 R# p
(CDR H3) of vertebrate antibodies typically contains a diverse loop of <15
: r8 j. B! B" famino acids and often provides a prominent role in binding antigen. Cows have 1 o/ b5 O1 Z5 Y
unusual CDR H3s of >60 amino acids with multiple cysteine residues. How these
, x# n2 X0 y: e4 ^unusual antibodies form and what their structural characteristics are have not # {, E4 b. H, g
been understood. Wang et al. (pp. 1379–1393) show that these antibodies form a & h7 {+ H4 ]/ i0 P8 E9 j$ e( E" N9 \
new structural domain comprised of “stalk” and “knob” features that are highly
/ Z. f6 I6 a0 H5 ediverse in amino acid content as well as disulfide patterns. They propose that
' H( b9 @" K. d" v- {bovine ultralong CDR H3 antibodies create antibody diversity by somatic 5 V& j2 k- e% e' K
diversification that creates unique disulfide patterns in the knob region. The 9 e* k" x# T: s7 R: c; N
cover shows the stalk and disulfide-bonded knob of a crystal structure of a cow
. n' H8 X- N; Kantibody (light-green, right) overlaid onto the oil painting “Red Calf Portrait”
( e: o/ g( R! ?- u1 y; m' Nby Denise Rich.8 i) Q  U5 J' B1 [; T. R" v

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懵懂干细胞

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