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CRYSTAL STRUCTURE OF MURINE CEACAM1A[1,4]: A CORONAVIRUS RECEPTOR AND CELL ADHESION MOLECULE IN THE CEA FAMILYCRYSTAL STRUCTURE OF MURINE CEACAM1A[1,4]: A CORONAVIRUS RECEPTOR AND CELL ADHESION MOLECULE IN THE CEA FAMILY
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCEACAM1 is a member of the carcinoembryonic antigen (CEA) family. Isoforms of murine CEACAM1 serve as receptors for mouse hepatitis virus (MHV), a murine coronavirus. Here we report the crystal structure of soluble murine sCEACAM1a[1,4], which is composed of two Ig-like domains and has MHV neutralizing activity. Its N-terminal domain has a uniquely folded CC' loop that encompasses key virus-binding residues. This is the first atomic structure of any member of the CEA family, and provides a prototypic architecture for functional exploration of CEA family members. We discuss the structural basis of virus receptor activities of murine CEACAM1 proteins, binding of Neisseria to human CEACAM1, and other homophilic and heterophilic interactions of CEA family members. Crystal structure of murine sCEACAM1a[1,4]: a coronavirus receptor in the CEA family.,Tan K, Zelus BD, Meijers R, Liu JH, Bergelson JM, Duke N, Zhang R, Joachimiak A, Holmes KV, Wang JH EMBO J. 2002 May 1;21(9):2076-86. PMID:11980704[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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