Structural highlights
Publication Abstract from PubMed
A three dimensional theoretical model of SP1 (stable protein 1), which is resistant to high temperature and biotic-stresses, is presented here. The model was generated by the application of homology modeling technique. The conformational rigidity imparted to the fold by the presence of hydrogen-bonded, C5, C7, C10 and C13 structures in the loop regions, multiple aromatic--aromatic interactions at the protein interior and on the surface, in addition to salt-links and hydrogen-bonds are primarily the major factors, responsible for the increased stability of protein. The putative protein family is characterized by motifs, E-x(0,1)-L-x-[AEGQS] and V-x(2,3)-L-x-[ADEGST] and the active site in the tertiary structure is formed by conserved aromatic and isoleucine clusters.
Structural features in the model of a thermostable and stress-resistant protein, SP1 from aspen.,Rathore RS, Narasimhamurthy T J Biomol Struct Dyn. 2004 Apr;21(5):651-5. PMID:14769057[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rathore RS, Narasimhamurthy T. Structural features in the model of a thermostable and stress-resistant protein, SP1 from aspen. J Biomol Struct Dyn. 2004 Apr;21(5):651-5. PMID:14769057
