1xgl: Difference between revisions

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{{STRUCTURE_1xgl|  PDB=1xgl  |  SCENE=  }}  
{{STRUCTURE_1xgl|  PDB=1xgl  |  SCENE=  }}  


'''HUMAN INSULIN DISULFIDE ISOMER, NMR, 10 STRUCTURES'''
===HUMAN INSULIN DISULFIDE ISOMER, NMR, 10 STRUCTURES===




==Overview==
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We have determined the structure of a metastable disulphide isomer of human insulin. Although not observed for proinsulin folding or insulin-chain recombination, the isomer retains ordered secondary structure and a compact hydrophobic core. Comparison with native insulin reveals a global rearrangement in the orientation of A- and B-chains. One face of the protein's surface is nevertheless in common between native and non-native structures. This face contains receptor-binding determinants, rationalizing the partial biological activity of the isomer. Structures of native and non-native disulphide isomers also define alternative three-dimensional templates. Threading of insulin-like sequences provide an experimental realization of the inverse protein-folding problem.
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{{ABSTRACT_PUBMED_7749917}}


==About this Structure==
==About this Structure==
1XGL is a [[Protein complex]] structure of sequences 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=1XGL OCA].  
1XGL is a [[Protein complex]] structure of sequences 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=1XGL OCA].  


==Reference==
==Reference==
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[[Category: Glucose metabolism]]
[[Category: Glucose metabolism]]
[[Category: Hormone]]
[[Category: Hormone]]
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