In this section
@article{Kotta-Loizou:2013:10.1016/j.bbapap.2013.01.006,
author = {Kotta-Loizou, I and Tsaousis, GN and Hamodrakas, SJ},
doi = {10.1016/j.bbapap.2013.01.006},
journal = {Biochim Biophys Acta},
pages = {798--807},
title = {Analysis of Molecular Recognition Features (MoRFs) in membrane proteins.},
url = {http://dx.doi.org/10.1016/j.bbapap.2013.01.006},
volume = {1834},
year = {2013}
}
TY - JOUR
AB - Molecular Recognition Features (MoRFs) are defined as short, intrinsically disordered regions in proteins that undergo disorder-to-order transition upon binding to their partners. As their name suggests, they are implicated in molecular recognition, which serves as the initial step for protein-protein interactions. Membrane proteins constitute approximately 30% of fully sequenced proteomes and are responsible for a wide variety of cellular functions. The aim of the current study was to identify and analyze MoRFs in membrane proteins. Two datasets of MoRFs, transmembrane and peripheral membrane protein MoRFs, were constructed from the Protein Data Bank, and sequence, structural and functional analysis was performed. Characterization of our datasets revealed their unique compositional biases and membrane protein MoRFs were categorized depending on their secondary structure after the interaction with their partners. Moreover, the position of transmembrane protein MoRFs in relation with the protein's topology was determined. Further studies were focused on functional analyses of MoRF-containing proteins and MoRFs' partners, associating them with protein binding, regulation and cell signaling, indicating half of them as putative hubs in protein-protein interaction networks. In conclusion, we provide insights into the disorder-based protein-protein interactions involving membrane proteins.
AU - Kotta-Loizou,I
AU - Tsaousis,GN
AU - Hamodrakas,SJ
DO - 10.1016/j.bbapap.2013.01.006
EP - 807
PY - 2013///
SN - 0006-3002
SP - 798
TI - Analysis of Molecular Recognition Features (MoRFs) in membrane proteins.
T2 - Biochim Biophys Acta
UR - http://dx.doi.org/10.1016/j.bbapap.2013.01.006
UR - https://www.ncbi.nlm.nih.gov/pubmed/23328413
VL - 1834
ER -
For any enquiries about the Fungal Science Network at Imperial, please contact: