1evr

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spinqualitylabelsall models 1evr, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

The structure of the resorcinol/insulin R6 hexamer

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The structures of three R(6) human insulin hexamers have been determined., Crystals of monoclinic m-cresol-insulin, monoclinic resorcinol-insulin and, rhombohedral m-cresol-insulin diffracted to 1. 9, 1.9 and 1.78 A, respectively, and have been refined to residuals of 0.195, 0.179 and, 0.200, respectively. In all three structures, a phenolic derivative is, found to occupy the phenolic binding site, where it forms hydrogen bonds, to the carbonyl O atom of CysA6 and the N atom of CysA11. Two additional, phenolic derivative binding sites were identified within or between, hexamers. The structures of all three hexamers are nearly identical, although a large displacement of the N-terminus of one B chain in both, monoclinic structures results from coordination to a sodium ion which is, located between symmetry-related hexamers. Other minor differences in, structure arise from differences in packing in the monoclinic cell, compared with the rhombohedral cell. Based upon the differences in, conformation of the GluB13 side chains in T(6), T(3)R(f)(3) and R(6), hexamers, the deprotonation of these side chains appears to be associated, with the T-->R conformational transition.

Disease

Known diseases associated with this structure: Diabetes mellitus, rare form OMIM:[176730], Hyperproinsulinemia, familial OMIM:[176730], MODY, one form OMIM:[176730]

About this Structure

1EVR is a Protein complex structure of sequences from [1] with ZN, CL, NA and RCO as ligands. Full crystallographic information is available from OCA.

Reference

R6 hexameric insulin complexed with m-cresol or resorcinol., Smith GD, Ciszak E, Magrum LA, Pangborn WA, Blessing RH, Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1541-8. PMID:11092919

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