2fyb
Crystal structure of the catalytic domain of the human beta1,4-galactosyltransferase mutant M339H in complex with Mn and UDP-galactose in open conformationCrystal structure of the catalytic domain of the human beta1,4-galactosyltransferase mutant M339H in complex with Mn and UDP-galactose in open conformation
DiseaseDisease
[B4GT1_HUMAN] Defects in B4GALT1 are the cause of congenital disorder of glycosylation type 2D (CDG2D) [MIM:607091]. CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation. They are characterized by under-glycosylated serum proteins. These multisystem disorders present with a wide variety of clinical features, such as disorders of the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
FunctionFunction
[B4GT1_HUMAN] The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix.
About this StructureAbout this Structure
2fyb is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Ramakrishnan B, Ramasamy V, Qasba PK. Structural snapshots of beta-1,4-galactosyltransferase-I along the kinetic pathway. J Mol Biol. 2006 Apr 14;357(5):1619-33. Epub 2006 Feb 9. PMID:16497331 doi:10.1016/j.jmb.2006.01.088