《细胞》[Cell]13年6月6日出版pdf全文

nero1981

; p) K+ ]" E7 DVolume 153, Issue 65 r) H& w* c- m7 k. T7 w; ^
On the cover: The complementarity determining region 3 of the heavy chain 2 Y, @. D$ @6 a: X- D
(CDR H3) of vertebrate antibodies typically contains a diverse loop of <15 5 T2 k/ g8 j3 F: t0 N8 Z
amino acids and often provides a prominent role in binding antigen. Cows have
  q  Y% F, w- |unusual CDR H3s of >60 amino acids with multiple cysteine residues. How these " g: ]" M& S" y# t5 d: \
unusual antibodies form and what their structural characteristics are have not 3 k0 ^' {2 z2 k2 X0 P5 V
been understood. Wang et al. (pp. 1379–1393) show that these antibodies form a
. V3 l/ q8 w1 e' ^new structural domain comprised of “stalk” and “knob” features that are highly * T& T  P, Q' k/ V
diverse in amino acid content as well as disulfide patterns. They propose that ' h9 P4 E$ s+ r! }
bovine ultralong CDR H3 antibodies create antibody diversity by somatic 3 y5 G: u) O4 Q4 A2 H0 S
diversification that creates unique disulfide patterns in the knob region. The 4 t6 _$ @8 ~# _0 V
cover shows the stalk and disulfide-bonded knob of a crystal structure of a cow - c; U% s( a. {! Z2 a4 q
antibody (light-green, right) overlaid onto the oil painting “Red Calf Portrait” $ e3 ?( r' [! X& i
by Denise Rich.3 n$ `! S% j1 T) m2 V

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yuheng

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exin11

nydfy

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zorro

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懵懂干细胞

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ljs

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ailingzheng

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illidancui

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redking2008

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