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2KJI

A divergent ins protein in c. elegans structurally resemble insulin and activates the human insulin receptor

Summary for 2KJI
Entry DOI10.2210/pdb2kji/pdb
Related4INS
DescriptorProbable insulin-like peptide beta-type 5 (1 entity in total)
Functional Keywordshormone, insulin like peptide, c. elegans, folding, ins-6, cleavage on pair of basic residues, disulfide bond, secreted
Biological sourceCaenorhabditis elegans (nematode)
Total number of polymer chains1
Total formula weight5304.07
Authors
Hua, Q.X.,Nakarawa, S.H.,Wilken, R.,Ramos, R.R.,Jia, W.H.,Bass, J.,Weiss, M.A. (deposition date: 2009-05-28, release date: 2009-06-16, Last modification date: 2024-10-16)
Primary citationHua, Q.X.,Nakagawa, S.H.,Wilken, J.,Ramos, R.R.,Jia, W.,Bass, J.,Weiss, M.A.
A divergent INS protein in Caenorhabditis elegans structurally resembles human insulin and activates the human insulin receptor.
Genes Dev., 17:826-831, 2003
Cited by
PubMed Abstract: Caenorhabditis elegans contains a family of putative insulin-like genes proposed to regulate dauer arrest and senescence. These sequences often lack characteristic sequence features of human insulin essential for its folding, structure, and function. Here, we describe the structure and receptor-binding properties of INS-6, a single-chain polypeptide expressed in specific neurons. Despite multiple nonconservative changes in sequence, INS-6 recapitulates an insulin-like fold. Although lacking classical receptor-binding determinants, INS-6 binds to and activates the human insulin receptor. Its activity is greater than that of an analogous single-chain human insulin analog.
PubMed: 12654724
DOI: 10.1101/gad.1058003
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2025-06-18公开中

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