How aberrant N-glycosylation can alter protein functionality and ligand binding: An atomistic view.

Castelli, Matteo; Yan, Pengrong; Rodina, Anna; Digwal, Chander S; Panchal, Palak; Chiosis, Gabriela; Moroni, Elisabetta; Colombo, Giorgio

Castelli, Matteo; Yan, Pengrong; Rodina, Anna; Digwal, Chander S; Panchal, Palak; Chiosis, Gabriela; Moroni, Elisabetta; Colombo, Giorgio.

Afiliación

Castelli M; Department of Chemistry, University of Pavia, via Taramelli 12, 27100 Pavia, Italy.
Yan P; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
Rodina A; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
Digwal CS; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
Panchal P; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
Chiosis G; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA; Department of Medicine, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA. Electronic address: chiosisg@mskcc.org.
Moroni E; SCITEC-CNR, via Mario Bianco 9, 20131 Milano, Italy. Electronic address: elisabetta.moroni@scitec.cnr.it.
Colombo G; Department of Chemistry, University of Pavia, via Taramelli 12, 27100 Pavia, Italy. Electronic address: g.colombo@unipv.it.

Structure ; 31(8): 987-1004.e8, 2023 08 03.

Article en En | MEDLINE | ID: mdl-37343552

Asunto(s)

Chaperonas Moleculares; Glicosilación; Ligandos; Chaperonas Moleculares/química; Conformación Proteica; Unión Proteica

Palabras clave

GRP94; aberrant protein conformations; allostery; disease; drug design; drug selectivity; epichaperomes; functional dynamics; glycosylation; post-translational modifications; protein assembly mutations

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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Chaperonas Moleculares Idioma: En Revista: Structure Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA / BIOTECNOLOGIA Año: 2023 Tipo del documento: Article País de afiliación: Italia

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