2aiy
From Proteopedia
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R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, 20 STRUCTURES
Overview
Crystallographic and NMR studies of insulin have revealed a highly, flexible molecule with a range of different aggregation and structural, states; the importance of these states for the function of the hormone is, still unclear. To address this question, we have studied the solution, structure of the insulin R6 symmetric hexamer using NMR spectroscopy., Structure determination of symmetric oligomers by NMR is complicated due, to 'symmetry ambiguity' between intra- and intermonomer NOEs, and between, different classes of intermonomer NOEs. Hence, to date, only two symmetric, tetramers and one symmetric pentamer (VTB, B subunit of verotoxin) have, been solved by NMR: there has been no other symmetric hexamer or, higher-order oligomer. Recently, we reported a solution structure for R6, ... [(full description)]
About this Structure
2AIY is a [Protein complex] structure of sequences from [[1]] with IPH as [ligand]. Full crystallographic information is available from [OCA].
Reference
Unraveling the symmetry ambiguity in a hexamer: calculation of the R6 human insulin structure., O'Donoghue SI, Chang X, Abseher R, Nilges M, Led JJ, J Biomol NMR. 2000 Feb;16(2):93-108. PMID:10723989
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