1lkq

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[[Image:1lkq.gif|left|200px]]
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{{Seed}}
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[[Image:1lkq.png|left|200px]]
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{{STRUCTURE_1lkq| PDB=1lkq | SCENE= }}
{{STRUCTURE_1lkq| PDB=1lkq | SCENE= }}
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'''NMR STRUCTURE OF HUMAN INSULIN MUTANT ILE-A2-GLY, VAL-A3-GLY, HIS-B10-ASP, PRO-B28-LYS, LYS-B29-PRO, 20 STRUCTURES'''
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===NMR STRUCTURE OF HUMAN INSULIN MUTANT ILE-A2-GLY, VAL-A3-GLY, HIS-B10-ASP, PRO-B28-LYS, LYS-B29-PRO, 20 STRUCTURES===
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==Overview==
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The A and B chains of insulin combine to form native disulfide bridges without detectable isomers. The fidelity of chain combination thus recapitulates the folding of proinsulin, a precursor protein in which the two chains are tethered by a disordered connecting peptide. We have recently shown that chain combination is blocked by seemingly conservative substitutions in the C-terminal alpha-helix of the A chain. Such analogs, once formed, nevertheless retain high biological activity. By contrast, we demonstrate here that chain combination is robust to non-conservative substitutions in the N-terminal alpha-helix. Introduction of multiple glycine substitutions into the N-terminal segment of the A chain (residues A1-A5) yields analogs that are less stable than native insulin and essentially without biological activity. (1)H NMR studies of a representative analog lacking invariant side chains Ile(A2) and Val(A3) (A chain sequence GGGEQCCTSICSLYQLENYCN; substitutions are italicized and cysteines are underlined) demonstrate local unfolding of the A1-A5 segment in an otherwise native-like structure. That this and related partial folds retain efficient disulfide pairing suggests that the native N-terminal alpha-helix does not participate in the transition state of the reaction. Implications for the hierarchical folding mechanisms of proinsulin and insulin-like growth factors are discussed.
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The line below this paragraph, {{ABSTRACT_PUBMED_12196530}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 12196530 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12196530}}
==About this Structure==
==About this Structure==
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1LKQ is a [[Protein complex]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LKQ OCA].
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1LKQ is a [[Protein complex]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LKQ OCA].
==Reference==
==Reference==
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[[Category: Human insulin]]
[[Category: Human insulin]]
[[Category: Mutant]]
[[Category: Mutant]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:00:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:20:12 2008''

Revision as of 18:20, 2 July 2008

Image:1lkq.png

Template:STRUCTURE 1lkq

NMR STRUCTURE OF HUMAN INSULIN MUTANT ILE-A2-GLY, VAL-A3-GLY, HIS-B10-ASP, PRO-B28-LYS, LYS-B29-PRO, 20 STRUCTURES

Template:ABSTRACT PUBMED 12196530

About this Structure

1LKQ is a Protein complex structure. Full experimental information is available from OCA.

Reference

Mechanism of insulin chain combination. Asymmetric roles of A-chain alpha-helices in disulfide pairing., Hua QX, Chu YC, Jia W, Phillips NF, Wang RY, Katsoyannis PG, Weiss MA, J Biol Chem. 2002 Nov 8;277(45):43443-53. Epub 2002 Aug 23. PMID:12196530

Page seeded by OCA on Wed Jul 2 21:20:12 2008

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