Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium

To understand how hCEACAM1 transitions between monomeric and dimeric states that are required for its activity, Gandhi et al. investigate hCEACAM1 homodimeric, monomeric, and transition states and their behavior in solution. This study suggests the flexibility of the GFCC’ face and its role in gover...

Full description

Bibliographic Details
Main Authors:	Amit K. Gandhi, Zhen-Yu J. Sun, Walter M. Kim, Yu-Hwa Huang, Yasuyuki Kondo, Daniel A. Bonsor, Eric J. Sundberg, Gerhard Wagner, Vijay K. Kuchroo, Gregory A. Petsko, Richard S. Blumberg
Format:	Article
Language:	English
Published:	Nature Publishing Group 2021-03-01
Series:	Communications Biology
Online Access:	https://doi.org/10.1038/s42003-021-01871-2

id	doaj-1e98a0721d5041b7bcee1fce74ebca91
record_format	Article
spelling	doaj-1e98a0721d5041b7bcee1fce74ebca912021-03-21T12:29:14ZengNature Publishing GroupCommunications Biology2399-36422021-03-014111410.1038/s42003-021-01871-2Structural basis of the dynamic human CEACAM1 monomer-dimer equilibriumAmit K. Gandhi0Zhen-Yu J. Sun1Walter M. Kim2Yu-Hwa Huang3Yasuyuki Kondo4Daniel A. Bonsor5Eric J. Sundberg6Gerhard Wagner7Vijay K. Kuchroo8Gregory A. Petsko9Richard S. Blumberg10Division of Gastroenterology, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical SchoolDepartment of Cancer Biology, Dana-Farber Cancer InstituteDivision of Gastroenterology, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical SchoolDivision of Gastroenterology, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical SchoolDivision of Gastroenterology, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical SchoolInstitute of Human Virology, University of Maryland School of Medicine, University of MarylandInstitute of Human Virology, University of Maryland School of Medicine, University of MarylandDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical SchoolEvergrande Center for Immunologic Diseases and Ann Romney Center for Neurologic Diseases, Harvard Medical School and Brigham and Women’s HospitalAnn Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women’s Hospital, Harvard Medical SchoolDivision of Gastroenterology, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical SchoolTo understand how hCEACAM1 transitions between monomeric and dimeric states that are required for its activity, Gandhi et al. investigate hCEACAM1 homodimeric, monomeric, and transition states and their behavior in solution. This study suggests the flexibility of the GFCC’ face and its role in governing the formation of hCEACAM1 dimers and selective heterodimers.https://doi.org/10.1038/s42003-021-01871-2
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Amit K. Gandhi Zhen-Yu J. Sun Walter M. Kim Yu-Hwa Huang Yasuyuki Kondo Daniel A. Bonsor Eric J. Sundberg Gerhard Wagner Vijay K. Kuchroo Gregory A. Petsko Richard S. Blumberg
spellingShingle	Amit K. Gandhi Zhen-Yu J. Sun Walter M. Kim Yu-Hwa Huang Yasuyuki Kondo Daniel A. Bonsor Eric J. Sundberg Gerhard Wagner Vijay K. Kuchroo Gregory A. Petsko Richard S. Blumberg Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium Communications Biology
author_facet	Amit K. Gandhi Zhen-Yu J. Sun Walter M. Kim Yu-Hwa Huang Yasuyuki Kondo Daniel A. Bonsor Eric J. Sundberg Gerhard Wagner Vijay K. Kuchroo Gregory A. Petsko Richard S. Blumberg
author_sort	Amit K. Gandhi
title	Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium
title_short	Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium
title_full	Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium
title_fullStr	Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium
title_full_unstemmed	Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium
title_sort	structural basis of the dynamic human ceacam1 monomer-dimer equilibrium
publisher	Nature Publishing Group
series	Communications Biology
issn	2399-3642
publishDate	2021-03-01
description	To understand how hCEACAM1 transitions between monomeric and dimeric states that are required for its activity, Gandhi et al. investigate hCEACAM1 homodimeric, monomeric, and transition states and their behavior in solution. This study suggests the flexibility of the GFCC’ face and its role in governing the formation of hCEACAM1 dimers and selective heterodimers.
url	https://doi.org/10.1038/s42003-021-01871-2
work_keys_str_mv	AT amitkgandhi structuralbasisofthedynamichumanceacam1monomerdimerequilibrium AT zhenyujsun structuralbasisofthedynamichumanceacam1monomerdimerequilibrium AT waltermkim structuralbasisofthedynamichumanceacam1monomerdimerequilibrium AT yuhwahuang structuralbasisofthedynamichumanceacam1monomerdimerequilibrium AT yasuyukikondo structuralbasisofthedynamichumanceacam1monomerdimerequilibrium AT danielabonsor structuralbasisofthedynamichumanceacam1monomerdimerequilibrium AT ericjsundberg structuralbasisofthedynamichumanceacam1monomerdimerequilibrium AT gerhardwagner structuralbasisofthedynamichumanceacam1monomerdimerequilibrium AT vijaykkuchroo structuralbasisofthedynamichumanceacam1monomerdimerequilibrium AT gregoryapetsko structuralbasisofthedynamichumanceacam1monomerdimerequilibrium AT richardsblumberg structuralbasisofthedynamichumanceacam1monomerdimerequilibrium
_version_	1724210495236341760

Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium

Similar Items