1xgl: Difference between revisions

Revision as of 15:00, 3 May 2008

HUMAN INSULIN DISULFIDE ISOMER, NMR, 10 STRUCTURES

OverviewOverview

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.

About this StructureAbout this Structure

1XGL is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a protein in a kinetic trap., Hua QX, Gozani SN, Chance RE, Hoffmann JA, Frank BH, Weiss MA, Nat Struct Biol. 1995 Feb;2(2):129-38. PMID:7749917 Page seeded by OCA on Sat May 3 15:00:16 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 [[Image:1xgl.jpg|left|200px]]
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 '''HUMAN INSULIN DISULFIDE ISOMER, NMR, 10 STRUCTURES'''
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 [[Category: Hua, Q X.]]
 [[Category: Weiss, M A.]]
-[[Category: glucose metabolism]]
+[[Category: Glucose metabolism]]
-[[Category: hormone]]
+[[Category: Hormone]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 15:00:16 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:49:19 2008''