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1sju

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[[Image:1sju.gif|left|200px]]
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{{STRUCTURE_1sju| PDB=1sju | SCENE= }}
{{STRUCTURE_1sju| PDB=1sju | SCENE= }}
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'''MINI-PROINSULIN, SINGLE CHAIN INSULIN ANALOG MUTANT: DES B30, HIS(B 10)ASP, PRO(B 28)ASP AND PEPTIDE BOND BETWEEN LYS B 29 AND GLY A 1, NMR, 20 STRUCTURES'''
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===MINI-PROINSULIN, SINGLE CHAIN INSULIN ANALOG MUTANT: DES B30, HIS(B 10)ASP, PRO(B 28)ASP AND PEPTIDE BOND BETWEEN LYS B 29 AND GLY A 1, NMR, 20 STRUCTURES===
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==Overview==
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Protein minimization highlights essential determinants of structure and function. Minimal models of proinsulin and insulin-like growth factor I contain homologous A and B domains as single-chain analogues. Such models (designated mini-proinsulin and mini-IGF-I) have attracted wide interest due to their native foldability but complete absence of biological activity. The crystal structure of mini-proinsulin, determined as a T3R3 hexamer, is similar to that of the native insulin hexamer. Here, we describe the solution structure of a monomeric mini-proinsulin under physiologic conditions and compare this structure to that of the corresponding two-chain analogue. The two proteins each contain substitutions in the B-chain (HisB10--&gt;Asp and ProB28--&gt;Asp) designed to destabilize self-association by electrostatic repulsion; the proteins differ by the presence or absence of a peptide bond between LysB29 and GlyA1. The structures are essentially identical, resembling in each case the T-state crystallographic protomer. Differences are observed near the site of cross-linking: the adjoining A1-A8 alpha-helix (variable among crystal structures) is less well-ordered in mini-proinsulin than in the two-chain variant. The single-chain analogue is not completely inactive: its affinity for the insulin receptor is 1500-fold lower than that of the two-chain analogue. Moreover, at saturating concentrations mini-proinsulin retains the ability to stimulate lipogenesis in adipocytes (native biological potency). These results suggest that a change in the conformation of insulin, as tethered by the B29-A1 peptide bond, optimizes affinity but is not integral to the mechanism of transmembrane signaling. Surprisingly, the tertiary structure of mini-proinsulin differs from that of mini-IGF-I (main-chain rms deviation 4.5 A) despite strict conservation of non-polar residues in their respective hydrophobic cores (side-chain rms deviation 4.9 A). Three-dimensional profile scores suggest that the two structures each provide acceptable templates for threading of insulin-like sequences. Mini-proinsulin and mini-IGF-I thus provide examples of homologous protein sequences encoding non-homologous structures.
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(as it appears on PubMed at http://www.pubmed.gov), where 9514738 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9514738}}
==About this Structure==
==About this Structure==
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1SJU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SJU OCA].
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1SJU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SJU OCA].
==Reference==
==Reference==
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[[Category: Hormone]]
[[Category: Hormone]]
[[Category: Signal]]
[[Category: Signal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:47:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:39:39 2008''

Revision as of 15:39, 28 July 2008

Image:1sju.jpg

Template:STRUCTURE 1sju

MINI-PROINSULIN, SINGLE CHAIN INSULIN ANALOG MUTANT: DES B30, HIS(B 10)ASP, PRO(B 28)ASP AND PEPTIDE BOND BETWEEN LYS B 29 AND GLY A 1, NMR, 20 STRUCTURES

Template:ABSTRACT PUBMED 9514738

About this Structure

1SJU is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Mini-proinsulin and mini-IGF-I: homologous protein sequences encoding non-homologous structures., Hua QX, Hu SQ, Jia W, Chu YC, Burke GT, Wang SH, Wang RY, Katsoyannis PG, Weiss MA, J Mol Biol. 1998 Mar 20;277(1):103-18. PMID:9514738

Page seeded by OCA on Mon Jul 28 18:39:39 2008

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