Desheptapeptide (B24 B30) insulin (DHPI), a virtually inactive insulin analog, has been crystallized in space group P2\-12\-12\-1 with two DHPI molecules in an asymmetric unit. The orientations and positions of the mo...Desheptapeptide (B24 B30) insulin (DHPI), a virtually inactive insulin analog, has been crystallized in space group P2\-12\-12\-1 with two DHPI molecules in an asymmetric unit. The orientations and positions of the molecules were determined by molecular replacement, and a structural model was built at 0.3 nm resolution. The current model shows that the two DHPI monomers are related by a non crystallographic 2 fold axis, nearly parallel to the crystallographic c axis. This structural feature complicated the determination of the orientation of the local 2 fold axis, which was later confirmed by analysing the diffraction data of DHPI crystals.展开更多
Desheptapeptide (B24—30) insulin (abbreviated as DHPI), prepared by the removal of the C-terminal amino acids of the B chain of insulin using limited enzymatic method, is an inactive analog of insulin. It can be crys...Desheptapeptide (B24—30) insulin (abbreviated as DHPI), prepared by the removal of the C-terminal amino acids of the B chain of insulin using limited enzymatic method, is an inactive analog of insulin. It can be crystallized in 30% acetone at pH 5.7 in platelet form. DHPI occupied a special position in those analogs with the Ctermini of the B chain shortened. Considering that the solution of the crystal strue-展开更多
The structure-function relationship of insulin to be understood at three-dimensional level has already been a challenging problem since the elucidation of fine crystal structures of insulin. Of course, it is a better ...The structure-function relationship of insulin to be understood at three-dimensional level has already been a challenging problem since the elucidation of fine crystal structures of insulin. Of course, it is a better experimental approach to such a problem that certain insulin-receptor complexes were prepared and their structures were展开更多
文摘Desheptapeptide (B24 B30) insulin (DHPI), a virtually inactive insulin analog, has been crystallized in space group P2\-12\-12\-1 with two DHPI molecules in an asymmetric unit. The orientations and positions of the molecules were determined by molecular replacement, and a structural model was built at 0.3 nm resolution. The current model shows that the two DHPI monomers are related by a non crystallographic 2 fold axis, nearly parallel to the crystallographic c axis. This structural feature complicated the determination of the orientation of the local 2 fold axis, which was later confirmed by analysing the diffraction data of DHPI crystals.
文摘Desheptapeptide (B24—30) insulin (abbreviated as DHPI), prepared by the removal of the C-terminal amino acids of the B chain of insulin using limited enzymatic method, is an inactive analog of insulin. It can be crystallized in 30% acetone at pH 5.7 in platelet form. DHPI occupied a special position in those analogs with the Ctermini of the B chain shortened. Considering that the solution of the crystal strue-
文摘The structure-function relationship of insulin to be understood at three-dimensional level has already been a challenging problem since the elucidation of fine crystal structures of insulin. Of course, it is a better experimental approach to such a problem that certain insulin-receptor complexes were prepared and their structures were
