skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Crystallization and Preliminary X-ray Analysis of the Human Long Myosin Light-Chain Kinase 1-Specific Domain IgCAM3

Journal Article · · Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Myosin light-chain kinase-dependent tight junction regulation is a critical event in inflammatory cytokine-induced increases in epithelial paracellular permeability. MLCK is expressed in human intestinal epithelium as two isoforms, long MLCK1 and long MLCK2, and MLCK1 is specifically localized to the tight junction, where it regulates paracellular permeability. The sole difference between these long MLCK splice variants is the presence of an immunoglobulin-like cell-adhesion molecule domain, IgCAM3, in MLCK1. To gain insight into the structure of the IgCAM3 domain, the IgCAM3 domain of MLCK1 has been expressed, purified and crystallized. Preliminary X-ray diffraction data were collected to 2.0 {angstrom} resolution and were consistent with the primitive trigonal space group P2{sub 1}2{sub 1}2{sub 1}.

Research Organization:
Brookhaven National Lab. (BNL), Upton, NY (United States)
Sponsoring Organization:
USDOE SC OFFICE OF SCIENCE (SC)
DOE Contract Number:
DE-AC02-98CH10886
OSTI ID:
1042193
Report Number(s):
BNL-97871-2012-JA; TRN: US201212%%604
Journal Information:
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 67, Issue 2; ISSN 1744-3091
Country of Publication:
United States
Language:
English