2QIU

Structure of Human Arg-Insulin

Summary for 2QIU

• Entry DOI: 10.2210/pdb2qiu/pdb
• Related: 1ZNI
• Descriptor: Insulin, ZINC ION, ... (4 entities in total)
• Functional Keywords: hormone, glucose utilisation, t3r3 conformation
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P01308 P01308
• Total number of polymer chains: 4
• Total formula weight: 12080.51

Authors

Sreekanth, R.,Pattabhi, V.,Rajan, S.S. (deposition date: 2007-07-05, release date: 2008-02-26, Last modification date: 2024-11-20)

Primary citation

Sreekanth, R.,Pattabhi, V.,Rajan, S.S.
Structural interpretation of reduced insulin activity as seen in the crystal structure of human Arg-insulin
Biochimie, 90:467-473, 2008

PubMed Abstract: The N-terminal glycine of the A-chain in insulin is reported to be one of the residues that binds to the insulin receptor. Modifications near this region lead to variations in the biological activity of insulin. One such modification viz., an addition of an arginine at the N-terminal A-chain, was reported to possess two-thirds the activity of native insulin. The crystal structure of 2 zinc human arg (A0) insulin has been elucidated to 2A resolution to understand the mechanism of reduction in insulin activity. A conformational transition from T6 to T3R3(f) and a decrease in the surface accessibility of residues in the so called receptor binding region have been observed. The presence of arginine has also induced distortions in the A chain N-terminal helix. The subtle conformational alterations like decrease in surface accessibility, alterations in the charge surface and changes in the relative orientation of the two helices in the A chain may be responsible for the reduction in activity.

PubMed: 18029081
DOI: 10.1016/j.biochi.2007.09.012

Experimental method

X-RAY DIFFRACTION (2 Å)