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Volume 153, Issue 6- L; Z0 Y2 Y) B1 [" X
On the cover: The complementarity determining region 3 of the heavy chain
8 l& I' A, \; C0 n! P9 g(CDR H3) of vertebrate antibodies typically contains a diverse loop of <15 / M, L% f0 R3 L6 |. K' S
amino acids and often provides a prominent role in binding antigen. Cows have
- I' [$ e/ D. O* J$ vunusual CDR H3s of >60 amino acids with multiple cysteine residues. How these , E3 D# J$ R+ F3 J, M2 n0 Z& S3 |
unusual antibodies form and what their structural characteristics are have not
- @0 g7 A; G: mbeen understood. Wang et al. (pp. 1379–1393) show that these antibodies form a 1 g9 i8 o% ?' i5 y3 B" F
new structural domain comprised of “stalk” and “knob” features that are highly ; k' z# O+ E& N8 ~0 Q0 H
diverse in amino acid content as well as disulfide patterns. They propose that
6 t- K& ]# T$ s% Kbovine ultralong CDR H3 antibodies create antibody diversity by somatic
# a8 w+ s, W4 U. c+ V$ M! Ndiversification that creates unique disulfide patterns in the knob region. The : y; H1 n9 g( H% U
cover shows the stalk and disulfide-bonded knob of a crystal structure of a cow
: u. _ w3 l! |, v! \antibody (light-green, right) overlaid onto the oil painting “Red Calf Portrait”
1 `8 ] ^1 A, m& ^. M3 P: Zby Denise Rich.4 b; _6 J8 M* ]4 R/ N0 d
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