The Structure of calnexin, an ER chaperone involved in quality control of protein folding.
The three-dimensional structure of the lumenal domain of the lectin-like chaperone calnexin determined to 2.9 A resolution reveals an extended 140 A arm inserted into a beta sandwich structure characteristic of legume lectins. The arm is composed of tandem repeats of two proline-rich sequence motifs which interact with one another in a head-to-tail fashion. Identification of the ligand binding site establishes calnexin as a monovalent lectin, providing insight into the mechanism by which the calnexin family of chaperones interacts with monoglucosylated glycoproteins.
Schrag
J D
JD
Biotechnology Research Institute, NRC, 6100 Royalmount Avenue, Montreal, Quebec H4P 2R2, Canada. joe@bri.nrc.ca
Bergeron
J J
JJ
Li
Y
Y
Borisova
S
S
Hahn
M
M
Thomas
D Y
DY
Cygler
M
M
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D037281:Calnexin; D037282:Calreticulin; D018360:Crystallography, X-Ray; D005947:Glucose / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012261:Ribonucleoproteins / Q000737:chemistry; D016415:Sequence Alignment
D002135:Calcium-Binding Proteins; D037282:Calreticulin; D008565:Membrane Proteins; D018832:Molecular Chaperones; D012261:Ribonucleoproteins; D037281:Calnexin; C087341:calmegin; D005947:Glucose; D002118:Calcium