Isolation and Structure Analysis of a SH3 Domain Protein from Monascus purpureus

DOI

10.2991/aeece-15.2015.147How to use a DOI?

Keywords

SH3 domain; homology modeling; cloning; Monascus purpureus; cDNA library.

Abstract

SH3 (Src homology 3) domain is a small modules units (~60 amino acids) that are important for the generation of protein-protein interactions in cellular signal transduction pathways. SH3 domains commonly bind to proline-rich sequences. Here, we explore the SH3 domain proteins in Monascus purpureus. A M. purpureus cDNA library was constructed, and the MpSH3 cDNA was isolated from the cDNA library by sequencing method. The cDNA was 1239 bp in length, contains a predicted 744 bp ORF that encodes 247 amino acids, the gene was designated MpSH3. The deduced amino acid sequence showed homology with SH3 domain proteins of fungi. A three-dimensional model of MpSH3 was built using homology modeling method. The 3D structure model of MpSH3 indicated that the domain is 52 residues long and is composed of five -strands, and has canonical RT, N-Src loops and 310-helix. The structure analysis implicated that the MpSH3 protein can mediate protein-proteins via recognition of proline-rich peptides.

Copyright

© 2015, the Authors. Published by Atlantis Press.

Open Access

This is an open access article distributed under the CC BY-NC license (http://creativecommons.org/licenses/by-nc/4.0/).

Download article (PDF)

TY  - CONF
AU  - Haoming Li
AU  - Lan Gao
PY  - 2015/09
DA  - 2015/09
TI  - Isolation and Structure Analysis of a SH3 Domain Protein from Monascus purpureus
BT  - Proceedings of the International Conference on Advances in Energy, Environment and Chemical Engineering
PB  - Atlantis Press
SP  - 727
EP  - 730
SN  - 2352-5401
UR  - https://doi.org/10.2991/aeece-15.2015.147
DO  - 10.2991/aeece-15.2015.147
ID  - Li2015/09
ER  -