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Properties of the C-terminal domain of 4.1 proteins.

Scott, Catherine, Phillips, Gareth W., Baines, Anthony J. (2001) Properties of the C-terminal domain of 4.1 proteins. European Journal of Biochemistry, 268 (13). pp. 3709-17. ISSN 0014-2956. (doi:10.1046/j.1432-1327.2001.02276.x) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:8640)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL:
http://dx.doi.org/10.1046/j.1432-1327.2001.02276.x

Abstract

At the C-terminus of all known 4.1 proteins is a sequence domain unique to these proteins, known as the C-terminal domain (CTD). Mammalian CTDs are associated with a growing number of protein-protein interactions, although such activities have yet to be associated with invertebrate CTDs. Mammalian CTDs are generally defined by sequence alignment as encoded by exons 18-21. Comparison of known vertebrate 4.1 proteins with invertebrate (Caenorhabditis elegans and Drosophila melanogaster) 4.1 proteins indicates that mammalian 4.1 exon 19 represents a vertebrate adaptation that extends the sequence of the CTD with a Ser/Thr-rich sequence. The CTD was first described as a 22/24-kDa domain by chymotryptic digestion of erythrocyte 4.1 (4.1R) [Leto, T.L. & Marchesi, V.T. (1984) J. Biol. Chem. 259, 4603-4608]. Here we show that in 4.1R the 22/24-kDa fragment is not stable but rapidly processed to a 15-kDa fragment by chymotrypsin. The 15-kDa fragment is extremely stable, being resistant to overnight digestion in chymotrypsin on ice. Analysis of this fragment indicates that it is derived from residues 709-858 (SwissProt accession no. P48193), and represents the CTD of 4.1R. The fragment behaves as a globular monomer in solution. Secondary-structure predictions indicate that this domain is composed of five or six beta strands with an alpha helix before the most C-terminal of these. Together these data indicate that the CTD probably represents an independent folding structure which has gained function since the divergence of vertebrates from invertebrates.

Item Type: Article
DOI/Identification number: 10.1046/j.1432-1327.2001.02276.x
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Anthony Baines
Date Deposited: 27 Oct 2008 14:00 UTC
Last Modified: 05 Nov 2024 09:41 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/8640 (The current URI for this page, for reference purposes)

University of Kent Author Information

Baines, Anthony J..

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