Structure of the N-terminal dimerization domain of CEACAM7

Acta Crystallographica. Section F, Structural Biology Communications
Daniel A BonsorEric J Sundberg

Abstract

CEACAM7 is a human cellular adhesion protein that is expressed on the surface of colon and rectum epithelial cells and is downregulated in colorectal cancers. It achieves cell adhesion through dimerization of the N-terminal IgV domain. The crystal structure of the N-terminal dimerization domain of CEACAM has been determined at 1.47 Å resolution. The overall fold of CEACAM7 is similar to those of CEACAM1 and CEACAM5; however, there are differences, the most notable of which is an insertion that causes the C'' strand to buckle, leading to the creation of a hydrogen bond in the dimerization interface. The Kdimerization for CEACAM7 determined by sedimentation equilibrium is tenfold tighter than that measured for CEACAM5. These findings suggest that the dimerization affinities of CEACAMs are modulated via sequence variation in the dimerization surface.

References

Dec 20, 1993·Journal of Molecular Biology·M C Lawrence, P M Colman
Nov 16, 2001·Biochemical and Biophysical Research Communications·T StreichertJ Brümmer
May 26, 2006·Nature Reviews. Immunology·Scott D Gray-Owen, Richard S Blumberg
Aug 25, 2006·Acta Crystallographica. Section D, Biological Crystallography·Alena FedarovichChristopher Davies
Aug 8, 2007·Journal of Molecular Biology·Evgeny Krissinel, Kim Henrick
Dec 19, 2007·Molecular Microbiology·Natalia KorotkovaSteve Matthews
Mar 12, 2008·Gynecologic Oncology·Behrang LitkouhiSamuel C Mok
May 9, 2008·Lung Cancer : Journal of the International Association for the Study of Lung Cancer·Björn Obrink
Jul 9, 2008·International Journal of Medical Microbiology : IJMM·Stefan PilsChristof R Hauck
Dec 17, 2008·Journal of Translational Medicine·Keith M Skubitz, Amy P N Skubitz
Jan 9, 2010·Acta Crystallographica. Section D, Biological Crystallography·Vincent B ChenDavid C Richardson
Jan 9, 2010·Acta Crystallographica. Section D, Biological Crystallography·Alexei Vagin, Alexei Teplyakov
Apr 13, 2010·Acta Crystallographica. Section D, Biological Crystallography·P EmsleyK Cowtan
Mar 4, 2011·Proceedings of the National Academy of Sciences of the United States of America·Jing ZhengPeter Dallos
Apr 5, 2011·Acta Crystallographica. Section D, Biological Crystallography·Martyn D WinnKeith S Wilson
Apr 5, 2011·Acta Crystallographica. Section D, Biological Crystallography·Garib N MurshudovAlexei A Vagin
Aug 2, 2013·Cancer Metastasis Reviews·Nicole Beauchemin, Azadeh Arabzadeh
Apr 20, 2014·PloS One·Bernhard B SingerHortense Slevogt
Jan 1, 1997·Methods in Enzymology·Zbyszek Otwinowski, Wladek Minor

❮ Previous
Next ❯

Citations

Feb 2, 2021·The EMBO Journal·Nina M van SorgeAlex J McCarthy
Jan 23, 2021·Clinical Cancer Research : an Official Journal of the American Association for Cancer Research·Deepak RajJohn F Marshall

❮ Previous
Next ❯

Methods Mentioned

BETA
X-ray
size-exclusion chromatography
Protein Crystallography
PISA
glycosylation

Software Mentioned

WinNonLin
HKL
MOLREP
PISA

Related Concepts

Related Feeds

Adhesion Molecules in Health and Disease

Cell adhesion molecules are a subset of cell adhesion proteins located on the cell surface involved in binding with other cells or with the extracellular matrix in the process called cell adhesion. In essence, cell adhesion molecules help cells stick to each other and to their surroundings. Cell adhesion is a crucial component in maintaining tissue structure and function. Discover the latest research on adhesion molecule and their role in health and disease here.