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2VK0

Crystal structure form ultalente insulin microcrystals

Summary for 2VK0
Entry DOI10.2210/pdb2vk0/pdb
Related1A7F 1AI0 1AIY 1B9E 1BEN 1EFE 1EV3 1EV6 1EVR 1FU2 1FUB 1G7A 1G7B 1GUJ 1HIQ 1HIS 1HIT 1HLS 1HTV 1HUI 1IOG 1IOH 1J73 1JCA 1JCO 1K3M 1KMF 1LKQ 1LPH 1MHI 1MHJ 1MSO 1OS3 1OS4 1Q4V 1QIY 1QIZ 1QJ0 1RWE 1SF1 1SJT 1T0C 1T1K 1T1P 1T1Q 1TRZ 1TYL 1TYM 1UZ9 1VKT 1W8P 1XDA 1XGL 1XW7 1ZEG 1ZEH 1ZNJ 2AIY 2C8Q 2C8R 2CEU 2H67 2HH4 2HHO 2HIU 2VJZ 3AIY 4AIY 5AIY
DescriptorINSULIN A CHAIN, INSULIN B CHAIN, ZINC ION, ... (5 entities in total)
Functional Keywordscarbohydrate metabolism, glucose metabolism, micro focus beamline, insulin, hormone, secreted, micro crystal, cleavage on pair of basic residues, disease mutation, diabetes mellitus
Biological sourceHOMO SAPIENS (HUMAN)
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Cellular locationSecreted: P01308 P01308
Total number of polymer chains4
Total formula weight12049.09
Authors
Wagner, A.,Diez, J.,Schulze-Briese, C.,Schluckebier, G. (deposition date: 2007-12-14, release date: 2008-09-16, Last modification date: 2024-10-16)
Primary citationWagner, A.,Diez, J.,Schulze-Briese, C.,Schluckebier, G.
Crystal Structure of Ultralente--A Microcrystalline Insulin Suspension.
Proteins, 74:1018-, 2009
Cited by
PubMed Abstract: Ultralente insulin has been one of the commercially most important insulin preparations in diabetes treatment over the last 50 years. It is a suspension of insulin microcrystals which dissolve slowly following subcutaneous injection. Because of the small crystal size of about 25 x 25 x 5 microm(3) the atomic structure has been elusive until now. Here we present the crystal structures from Ultralente and their precursor microcrystals from the industrial manufacturing process. During this process insulin undergoes a conformational change within the microcrystals. Both structures show canonical folding of the insulin molecules but exhibit a number of new features when compared with other insulin structures. Surprisingly, we found that the Ultralente crystals bind the conservation agent methylparaben, which slows down dissolution of the crystals and thus contributes to the long duration of action.
PubMed: 18767151
DOI: 10.1002/PROT.22213
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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