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A T cell receptor CDR3beta loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex.

Abstract：

:The elongated complementary-determining region (CDR) 3beta found in the unliganded KB5-C20 TCR protrudes from the antigen binding site and prevents its docking onto the peptide/MHC (pMHC) surface according to a canonical diagonal orientation. We now present the crystal structure of a complex involving the KB5-C20 TCR and an octapeptide bound to the allogeneic H-2K(b) MHC class I molecule. This structure reveals how a tremendously large CDR3beta conformational change allows the KB5-C20 TCR to adapt to the rather constrained pMHC surface and achieve a diagonal docking mode. This extreme case of induced fit also shows that TCR plasticity is primarily restricted to CDR3 loops and does not propagate away from the antigen binding site.

journal_name

Immunity

journal_title

Immunity

authors

Reiser JB,Grégoire C,Darnault C,Mosser T,Guimezanes A,Schmitt-Verhulst AM,Fontecilla-Camps JC,Mazza G,Malissen B,Housset D

doi

10.1016/s1074-7613(02)00288-1

keywords:

subject

Has Abstract

pub_date

2002-03-01 00:00:00

pages

345-54

issue

3

eissn

1074-7613

issn

1097-4180

pii

S1074-7613(02)00288-1

journal_volume

16

pub_type

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