5ena

Xray crystal structure of isotope-labeled human insulin

spinqualitylabelsall models 5ena, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ena is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 5en9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Disease [INS_HUMAN] Defects in INS are the cause of familial hyperproinsulinemia (FHPRI) [MIM:176730]. Defects in INS are a cause of diabetes mellitus insulin-dependent type 2 (IDDM2) [MIM:125852]. IDDM2 is a multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical fetaures are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. Defects in INS are a cause of diabetes mellitus permanent neonatal (PNDM) [MIM:606176]. PNDM is a rare form of diabetes distinct from childhood-onset autoimmune diabetes mellitus type 1. It is characterized by insulin-requiring hyperglycemia that is diagnosed within the first months of life. Permanent neonatal diabetes requires lifelong therapy. Defects in INS are a cause of maturity-onset diabetes of the young type 10 (MODY10) [MIM:613370]. MODY10 is a form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease. Function [INS_HUMAN] Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. Publication Abstract from PubMed As a part of a program aimed towards the study of the dynamics of human insulin protein dimer formation using two dimensional infra red (2D-IR) spectroscopy, we have used total chemical synthesis to prepare stable isotope labeled [(1-13C=18O)PheB24)]human insulin, via [(1-13C=18O)PheB24)]ester insulin as a key intermediate product that facilitates folding of the synthetic protein molecule (see accompanying article). In the present paper, we describe the crystal structure of the synthetic isotope-labeled ester insulin intermediate and the product synthetic human insulin, and our observations on hexamer formation with these two protein molecules in the absence of phenol derivatives and/or Zn metal ions. We also describe and discuss the fractional crystallization of quasi-racemic protein mixtures containing each of these two synthetic proteins. Crystallization of enantiomerically pure proteins from quasi-racemic mixtures: structure determination by X-ray diffraction of isotope-labeled ester insulin and human insulin.,Kent S, Mandal K, Dhayalan B, Avital-Shmilovici M, Tokmakoff A Chembiochem. 2015 Dec 28. doi: 10.1002/cbic.201500600. PMID:26707939 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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