title: Comparative sequence-structure analysis of Aves insulin.
abstract: Normal blood glucose level depends on the availability of insulin and its ability to bind insulin receptor (IR) that regulates the downstream signaling pathway. Insulin sequence and blood glucose level usually vary among animals due to species specificity. The study of genetic variation of insulin, blood glucose level and diabetics symptoms development in Aves is interesting because of its optimal high blood glucose level than mammals. Therefore, it is of interest to study its evolutionary relationship with other mammals using sequence data. Hence, we compiled 32 Aves insulin from GenBank to compare its sequence-structure features with phylogeny for evolutionary inference. The analysis shows long conserved motifs (about 14 residues) for functional inference. These sequences show high leucine content (20%) with high instability index (>40). Amino acid position 11, 14, 16 and 20 are variable that may have contribution to binding to IR. We identified functionally critical variable residues in the dataset for possible genetic implication. Structural models of these sequences were developed for surface analysis towards functional representation. These data find application in the understanding of insulin function across species.
authors.affiliation: Pharmacogenomics Lab, Department of Pharmacology, Faculty of Medicine, University of Malaya, 50603 Kuala Lumpur, Malaysia.
authors.forename: Md Mirazul
authors.initials: MM
authors.lastname: Islam
authors.affiliation: Pharmacogenomics Lab, Department of Pharmacology, Faculty of Medicine, University of Malaya, 50603 Kuala Lumpur, Malaysia.
authors.forename: M
authors.initials: M
authors.lastname: Aktaruzzaman
authors.affiliation: Pharmacogenomics Lab, Department of Pharmacology, Faculty of Medicine, University of Malaya, 50603 Kuala Lumpur, Malaysia.
authors.forename: Zahurin
authors.initials: Z
authors.lastname: Mohamed
keywords: Aves Insulin; blood glucose level; physic-chemical properties; sequence-structure analysis
references.citation: J Wildl Dis. 2011 Jul;47(3):523-9
references.pmid: 21719817
references.citation: Eur J Biochem. 1994 May 1;221(3):1127-32
references.pmid: 8181471
references.citation: Nature. 2001 Dec 13;414(6865):799-806
references.pmid: 11742412
references.citation: Diabetes. 2006 Dec;55(12):3201-13
references.pmid: 17130462
references.citation: Bioinformation. 2013;9(1):42-8
references.pmid: 23390343
references.citation: J Wildl Dis. 1978 Oct;14(4):479-81
references.pmid: 739587
references.citation: Bioinformation. 2013 Jun 29;9(11):572-6
references.pmid: 23888098
references.citation: Diabetes Care. 2012 Aug;35(8):1746-8
references.pmid: 22699291
references.citation: Comput Appl Biosci. 1995 Dec;11(6):681-4
references.pmid: 8808585
references.citation: Endocr Rev. 2001 Dec;22(6):818-35
references.pmid: 11739335
references.citation: Nature. 1982 Aug 12;298(5875):667-9
references.pmid: 6178977
references.citation: Annu Rev Physiol. 2003;65:313-32
references.pmid: 12471165
references.citation: JAMA. 1965 Nov 8;194(6):587-92
references.pmid: 5897230