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. ~( H' Y0 U/ @, c6 L. nVolume 153, Issue 6
# b# l7 \, T1 c8 q0 L) xOn the cover: The complementarity determining region 3 of the heavy chain
' Q! S5 t* d' K3 N+ z$ K/ S( A(CDR H3) of vertebrate antibodies typically contains a diverse loop of <15 5 \" p n/ c, J3 x2 p; s. R
amino acids and often provides a prominent role in binding antigen. Cows have
' a8 B+ g x4 ~. x- nunusual CDR H3s of >60 amino acids with multiple cysteine residues. How these 4 ]* D' Z( [1 c' F4 v8 _2 Q
unusual antibodies form and what their structural characteristics are have not
/ p& _$ \4 N# m2 K7 m; {been understood. Wang et al. (pp. 1379–1393) show that these antibodies form a 8 s9 ^ ]" e$ F4 j/ j, \8 X
new structural domain comprised of “stalk” and “knob” features that are highly
$ _2 ^4 c; k4 q8 p6 K; wdiverse in amino acid content as well as disulfide patterns. They propose that - H$ A: Z8 S0 r/ G% x3 m, p
bovine ultralong CDR H3 antibodies create antibody diversity by somatic
$ p9 @/ k5 j$ a4 a2 z8 t _3 J9 |diversification that creates unique disulfide patterns in the knob region. The / K# _4 w' F* ~" D
cover shows the stalk and disulfide-bonded knob of a crystal structure of a cow ' g4 F" O8 _. d$ h3 ~8 F' G
antibody (light-green, right) overlaid onto the oil painting “Red Calf Portrait” 2 H6 K2 G( |: M3 @5 @, G
by Denise Rich.9 w& ^4 x3 Z0 S# }6 o+ b9 }' a: e
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发表于 2013-6-7 07:30
发表于 2013-6-7 07:57
