About this site

Coiled-coil domains are characterized by a heptad repeat pattern in which residues in the first and fourth position are hydrophobic, and residues in the fifth and seventh position are predominantly charged or polar. This pattern can be used by computational methods, such as MultiCoil, to predict coiled-coil domains in amino acid sequences.

In animals and yeast, the coiled-coil motif has been identified in a variety of proteins associated with the cytoskeleton, the golgi, centromers, centrosomes, the nuclear matrix, and chromatin. These proteins play an important role in the association of functional proteins (e.g signal transduction components) with the solid-state components of the cell.

In contrast to animals and yeast, almost no long coiled-coil proteins have been investigated in plants.

About the ARABI-COIL database

In collaboration with the "Ohio Supercomputer Center (OSC)", we established the algorithm Multicoil on a 32 processor SGI Origin 2000 system 2003. We have screened the 26,945 annotated Arabidopsis open reading frames for coiled-coil domains. About 300 proteins with long coiled-coil domains were further analyzed for putative function and localization. With the ARABI-COIL database, we share the results of our analysis with the research community.

Reference:

Annkatrin Rose, Sankaraganesh Manikantan, Shannon J. Schraegle, Michael A. Maloy, Eric A. Stahlberg, and Iris Meier (2004). Genome-wide Identification of Arabidopsis Coiled-Coil Proteins and Establishment of the ARABI-COIL Database. Plant Physiol. 134, 927-939.

A.R., I.M.: Department of Plant Biology and Plant Biotechnology Center, The Ohio State University, 1060 Carmack Road, Columbus, OH 43210, USA

S.M., S.J.S., M.A.M., E.A.S.: Ohio Supercomputer Center, 1224 Kinnear Road, Columbus, OH 43212, USA
Current correspondence should be directed to E.A.S at Wittenberg University

Abstract at NCBI PubMed

The ARABI-COIL database was made possible with support from the National Science Foundation Project 2010 and the Ohio Supercomputer Center.

Contact:

Meier Lab OSC Bioinformatics Resource Group

--- DISCLAIMER ---

COILED-COIL (http://www.coiled-coil.org) is a collaborative project investigating the relationship of coiled-coil protein structure with biological activity in plants. Funded by the National Science Foundation (NSF 0209339) as part of the 2010 effort, the project combines computational and experimental results to create a protein structure information resource. Computational and operational support are also provided by the Ohio State University Plant Biology Department and the Ohio Supercomputer Center.
Any opinions, findings, and conclusions or recommendations expressed in this material are those of the authors and do not necessarily reflect the views of the National Science Foundation or the Ohio State University.