1uz9
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(New page: 200px<br /> <applet load="1uz9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uz9, resolution 1.6Å" /> '''CRYSTALLOGRAPHIC AND...)
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Revision as of 15:41, 29 October 2007
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CRYSTALLOGRAPHIC AND SOLUTION STUDIES OF N-LITHOCHOLYL INSULIN: A NEW GENERATION OF PROLONGED-ACTING INSULINS.
Overview
The addition of specific bulky hydrophobic groups to the insulin molecule, provides it with affinity for circulating serum albumin and enables it to, form soluble macromolecular complexes at the site of subcutaneous, injection, thereby securing slow absorption of the insulin analogue into, the blood stream and prolonging its half-life once there. N-Lithocholic, acid acylated insulin [Lys(B29)-lithocholyl des-(B30) human insulin] has, been crystallized and the structure determined by X-ray crystallography at, 1.6 A resolution to explore the molecular basis of its assembly. The unit, cell in the crystal consists of an insulin hexamer containing two zinc, ions, with two m-cresol molecules bound at each dimer-dimer interface, stabilizing an R(6) conformation. Six covalently bound lithocholyl ... [(full description)]
About this Structure
1UZ9 is a [Protein complex] structure of sequences from [[1]] with ZN, CL, CRS and UZ9 as [ligands]. Full crystallographic information is available from [OCA].
Reference
Crystallographic and solution studies of N-lithocholyl insulin: a new generation of prolonged-acting human insulins., Whittingham JL, Jonassen I, Havelund S, Roberts SM, Dodson EJ, Verma CS, Wilkinson AJ, Dodson GG, Biochemistry. 2004 May 25;43(20):5987-95. PMID:15147182
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