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Volume 153, Issue 6
/ H1 E# _! \) W$ T, EOn the cover: The complementarity determining region 3 of the heavy chain
' I5 D" t; ~! S& N0 R2 ?6 X! Y8 k(CDR H3) of vertebrate antibodies typically contains a diverse loop of <15 2 p1 q) Y7 ?( J) S+ `
amino acids and often provides a prominent role in binding antigen. Cows have
& S- h3 q+ R$ O: O' ^# @unusual CDR H3s of >60 amino acids with multiple cysteine residues. How these ) Y( d! o6 U& z
unusual antibodies form and what their structural characteristics are have not " [ j5 c: j) w$ Y! T
been understood. Wang et al. (pp. 1379–1393) show that these antibodies form a
9 E U5 Y' p; w( r* `$ l, Lnew structural domain comprised of “stalk” and “knob” features that are highly , u* `' P5 ~5 c1 m- |
diverse in amino acid content as well as disulfide patterns. They propose that # P+ h; @; b( L9 }! F: G! p5 a0 i8 p% h
bovine ultralong CDR H3 antibodies create antibody diversity by somatic
9 K$ I+ B l" D9 e% j9 m- H: ~' [diversification that creates unique disulfide patterns in the knob region. The 2 C9 @0 L* W, G) f' j8 T7 {: x% [
cover shows the stalk and disulfide-bonded knob of a crystal structure of a cow
. B( b* `" ~9 E' }3 D" Wantibody (light-green, right) overlaid onto the oil painting “Red Calf Portrait”
' k& j- {6 j3 Q% a$ h! s/ ^by Denise Rich.
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