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1 H‐NMR analysis of CD3‐ϵ reveals the presence of turn‐helix structures around the ITAM motif in an otherwise random coil cytoplasmic tail

1 H‐NMR analysis of CD3‐ϵ reveals the presence of turn‐helix structures around the ITAM motif in... 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 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biopolymers Wiley

1 H‐NMR analysis of CD3‐ϵ reveals the presence of turn‐helix structures around the ITAM motif in an otherwise random coil cytoplasmic tail

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References (33)

Publisher
Wiley
Copyright
Copyright © 1997 John Wiley & Sons, Inc.
ISSN
0006-3525
eISSN
1097-0282
DOI
10.1002/(SICI)1097-0282(199707)42:1<75::AID-BIP7>3.0.CO;2-Z
pmid
9209158
Publisher site
See Article on Publisher Site

Abstract

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

Journal

BiopolymersWiley

Published: Jul 1, 1997

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