《细胞》[Cell]13年6月6日出版pdf全文

nero1981

7 Q' e4 G; Z1 Q0 z) |& Y6 Y( `Volume 153, Issue 6+ ]3 @1 G" F- b3 R' S5 F: s
On the cover: The complementarity determining region 3 of the heavy chain
6 ^0 s' F- M. W: C2 x; Q(CDR H3) of vertebrate antibodies typically contains a diverse loop of <15
& n( ^* m2 H9 k3 W- {1 f* P# _5 {amino acids and often provides a prominent role in binding antigen. Cows have
0 ?. w& y8 x+ X. o/ hunusual CDR H3s of >60 amino acids with multiple cysteine residues. How these
+ y, L+ y; B5 Q3 Z* ?7 r0 b0 [1 gunusual antibodies form and what their structural characteristics are have not % Y7 h  t  y" q( m1 ]+ A
been understood. Wang et al. (pp. 1379–1393) show that these antibodies form a * A  U9 I( ]8 r4 |* X; V; n4 e1 A+ z
new structural domain comprised of “stalk” and “knob” features that are highly
' R: _" d1 k+ t, }! s* L- W0 Gdiverse in amino acid content as well as disulfide patterns. They propose that 5 b) S0 {" z& ]/ o" _% o
bovine ultralong CDR H3 antibodies create antibody diversity by somatic 4 T- ?4 [9 F% G. F+ P
diversification that creates unique disulfide patterns in the knob region. The , v, v7 c& ?$ C, _
cover shows the stalk and disulfide-bonded knob of a crystal structure of a cow
8 n% o$ k- `) J# L, j5 Vantibody (light-green, right) overlaid onto the oil painting “Red Calf Portrait” 3 l9 l* I  W# J4 H4 G) G
by Denise Rich.% {& p$ k( [; w4 V

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hmhy

支持一下吧  

biopxl

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tuanzi

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mk990

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顶一个先  

大小年

世界上那些最容易的事情中，拖延时间最不费力。