TY - JOUR
T1 - Dual role of interactions between membranous and soluble portions of helical membrane receptors for folding and signaling
AU - Klein-Seetharaman, Judith
N1 - Funding Information:
Work from my laboratory that is discussed in this review was funded by NSF grant 0225636, NIH-NLM grant 1R01LM007994 and the Sofya Kovalevskaya Prize from the Humboldt-Foundation/Zukunftsinvestitionsprogramm der Bundesregierung Deutschland.
PY - 2005/4
Y1 - 2005/4
N2 - Dramatic advances in the understanding of the molecular mechanisms of membrane receptor activation for several prototypic members of different families of receptors have taken place during the past 2-3 years. The new structures of receptor fragments or full-length receptors in different conformations have been reviewed previously in light of the large bodies of available structure-function data. However, in this article, we will compare, among different receptor families, the emerging paradigms for conformational changes during signaling. Recent advances in the understanding of membrane-protein folding suggest that these paradigms are closely related to those that describe the folding and structural stability of membrane proteins. These relate in particular to long-range interactions not only within but also between soluble or membrane-embedded parts of proteins.
AB - Dramatic advances in the understanding of the molecular mechanisms of membrane receptor activation for several prototypic members of different families of receptors have taken place during the past 2-3 years. The new structures of receptor fragments or full-length receptors in different conformations have been reviewed previously in light of the large bodies of available structure-function data. However, in this article, we will compare, among different receptor families, the emerging paradigms for conformational changes during signaling. Recent advances in the understanding of membrane-protein folding suggest that these paradigms are closely related to those that describe the folding and structural stability of membrane proteins. These relate in particular to long-range interactions not only within but also between soluble or membrane-embedded parts of proteins.
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U2 - 10.1016/j.tips.2005.02.009
DO - 10.1016/j.tips.2005.02.009
M3 - Review article
C2 - 15808342
AN - SCOPUS:15944387765
SN - 0165-6147
VL - 26
SP - 183
EP - 189
JO - Trends in Pharmacological Sciences
JF - Trends in Pharmacological Sciences
IS - 4
ER -