In:
Journal of Bioinformatics and Computational Biology, World Scientific Pub Co Pte Ltd, Vol. 09, No. 04 ( 2011-08), p. 471-488
Abstract:
Solute transporters (STs) are an important subgroup of integral membrane proteins that facilitate the translocation of a diverse range of solutes such as sugars, amino acids, and neurotransmitters across cell membranes. Sequence analysis indicates that STs possess multiple stretches of hydrophobic-rich amino acids that are organized into the transmembrane domains (TMDs) of the functional protein, but exactly how the correct spatial arrangement of these domains is achieved remains a challenging problem. We hypothesized that perhaps differences in interdomain hydrophobicity might play some role in this process. To test this hypothesis, we generated a heptadic model of the alpha helix and mapped the average hydrophobicities (coaxial) and hydrophobic moments (radial) of 108 TMDs found in 9 different human ST proteins. Our results, taken together with earlier work from other groups, suggest that spatial patterns of hydrophobicity found in TMDs 1 and 2 are consistent with a role for these domains in the initial anchoring of the nascent ST protein to the endoplasmic reticulum (ER), as it emerges from the ribosome complex and perhaps in the subsequent spatial organisation of STs.
Type of Medium:
Online Resource
ISSN:
0219-7200
,
1757-6334
DOI:
10.1142/S0219720011005367
Language:
English
Publisher:
World Scientific Pub Co Pte Ltd
Publication Date:
2011
SSG:
12
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