2g8e

From Proteopedia
Revision as of 11:54, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="2g8e" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g8e, resolution 2.25Å" /> '''Calpain 1 proteolyti...)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search
File:2g8e.gif


2g8e, resolution 2.25Å

Drag the structure with the mouse to rotate

Calpain 1 proteolytic core in complex with SNJ-1715, a cyclic hemiacetal-type inhibitor

OverviewOverview

Calpains are intracellular calcium-activated cysteine proteases whose, unregulated proteolysis following the loss of calcium homeostasis can lead, to acute degeneration during ischemic episodes and trauma, as well as, Alzheimer's disease and cataract formation. The determination of the, crystal structure of the proteolytic core of mu-calpain (muI-II) in a, calcium-bound active conformation has made structure-guided design of, active site inhibitors feasible. We present here high-resolution crystal, structures of rat muI-II complexed with two reversible calpain-specific, inhibitors employing cyclic hemiacetal (SNJ-1715) and alpha-ketoamide, (SNJ-1945) chemistries that reveal new details about the interactions of, inhibitors with this enzyme. The SNJ-1715 complex confirms that the free, aldehyde is the reactive species of the cornea-permeable cyclic, hemiacetal. The alpha-ketoamide warhead of SNJ-1945 binds with the, hydroxyl group of the tetrahedral adduct pointing toward the catalytic, histidine rather than the oxyanion hole. The muI-II-SNJ-1945 complex shows, residue Glu261 displaced from the S1' site by the inhibitor, resulting in, an extended "open" conformation of the domain II gating loop and an, unobstructed S1' site. This conformation offers an additional template for, structure-based drug design extending to the primed subsites. An important, role for the highly conserved Glu261 is proposed.

About this StructureAbout this Structure

2G8E is a Single protein structure of sequence from Rattus norvegicus with CA, D5G and MES as ligands. Active as Calpain-1, with EC number 3.4.22.52 Full crystallographic information is available from OCA.

ReferenceReference

Calpain inhibition by alpha-ketoamide and cyclic hemiacetal inhibitors revealed by X-ray crystallography., Cuerrier D, Moldoveanu T, Inoue J, Davies PL, Campbell RL, Biochemistry. 2006 Jun 20;45(24):7446-52. PMID:16768440

Page seeded by OCA on Wed Nov 21 11:01:44 2007

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA