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10.1002/(SICI)1097-0282(199707)42:1<75::AID-BIP7>3.3.CO;2-S The conformation adopted in solution by the cytoplasmic tail of CD3‐ϵ has been analyzed by 1H‐nmr. The cytoplasmic tail is mostly random coil except for the amino acids conforming the immunoreceptor tyrosine‐based activation motif (ITAM), YxxL/IxxxxxxxY xxL. Although the N‐terminal Y xxL sequence of the motif is poorly folded, adopting 6‐residue turn‐like conformations with the Tyr side chain in two different orientations, the C‐terminal Y xxL sequence is placed in a more complex structure involving a set of nonclassical α‐helix turns and β‐turns that comprises 11 amino acids. This structure is not modified by phosphorylation of the tyrosine residue. The differences in the conformation adopted around the two tyrosines of the ITAM motif suggest that they may play different roles pertaining to either binding signal transducing proteins or, alternatively, proteins involved in other processes such as endoplasmic reticulum location. © 1997 John Wiley & Sons, Inc. Biopoly 42: 75–88, 1997
Biopolymers – Wiley
Published: Jul 1, 1997
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