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Q% ^5 t8 c5 K ~0 n YVolume 153, Issue 6) }# K6 K2 ^ q" Q
On the cover: The complementarity determining region 3 of the heavy chain ! _. Z% s8 i+ w a& [# `4 F
(CDR H3) of vertebrate antibodies typically contains a diverse loop of <15
& m5 B3 h' W# S/ x- S5 _amino acids and often provides a prominent role in binding antigen. Cows have * `$ T$ N8 j$ v4 {
unusual CDR H3s of >60 amino acids with multiple cysteine residues. How these ) P: d1 x8 y# W- n" d, t( Q6 L" Z
unusual antibodies form and what their structural characteristics are have not
4 t9 ~$ M0 s" V# sbeen understood. Wang et al. (pp. 1379–1393) show that these antibodies form a
) [4 Q+ \8 s0 v+ y& y8 C# Anew structural domain comprised of “stalk” and “knob” features that are highly s, X% S5 \5 @$ z/ F. l
diverse in amino acid content as well as disulfide patterns. They propose that
+ W, M# R `5 M) Q: D! t( Qbovine ultralong CDR H3 antibodies create antibody diversity by somatic 8 F! I4 U' Y' x& e, m+ J A
diversification that creates unique disulfide patterns in the knob region. The
$ ^; w# @; }$ b* {) }. [3 mcover shows the stalk and disulfide-bonded knob of a crystal structure of a cow 8 ^0 d* h' k* r# h$ o
antibody (light-green, right) overlaid onto the oil painting “Red Calf Portrait” 6 F s/ y% Q9 e2 {: K+ I
by Denise Rich.
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发表于 2013-6-7 07:30
发表于 2013-6-7 07:57
