1LPH

LYS(B28)PRO(B29)-HUMAN INSULIN

Summary for 1LPH

• Entry DOI: 10.2210/pdb1lph/pdb
• Descriptor: INSULIN, ZINC ION, PHENOL, ... (6 entities in total)
• Functional Keywords: insulin analogue, hormone, glucose metabolism
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P01308 P01308
• Total number of polymer chains: 4
• Total formula weight: 11895.68

Authors

Ciszak, E.,Beals, J.M.,Frank, B.H.,Baker, J.C.,Carter, N.D.,Smith, G.D. (deposition date: 1995-04-19, release date: 1996-06-20, Last modification date: 2024-11-13)

Primary citation

Ciszak, E.,Beals, J.M.,Frank, B.H.,Baker, J.C.,Carter, N.D.,Smith, G.D.
Role of C-terminal B-chain residues in insulin assembly: the structure of hexameric LysB28ProB29-human insulin.
Structure, 3:615-622, 1995

PubMed Abstract: LysB28ProB29-human insulin (Humalog), a fully potent insulin analog in which the prolyl, lysyl sequence at the C-terminal end of the B-chain is inverted, exhibits a decreased association of monomers to dimers leading to rapid in vivo absorption. This provides important benefits for the insulin-requiring diabetic. In spite of its monomeric nature, LysB28ProB29-human insulin can exist as a discrete hexameric structure in the presence of both zinc and phenol. Studies of the crystal structure of LysB28ProB29-human insulin in a hexameric complex were initiated to gain a molecular understanding of the effect of the sequence inversion on the analog's self-association properties and, consequently, its in vivo efficacy.

PubMed: 8590022
DOI: 10.1016/S0969-2126(01)00195-2

Experimental method

X-RAY DIFFRACTION (2.3 Å)