Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIII.

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Citation

Wigren E, Bourhis JM, Kursula I, Guy JE, Lindqvist Y

Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIII.

FEBS Lett. 2010 Mar 5;584(5):878-82. doi: 10.1016/j.febslet.2010.02.009. Epub 2010 Feb 9.

PubMed ID
20138881 [ View in PubMed
]
Abstract

LMAN1 is a glycoprotein receptor, mediating transfer from the ER to the ER-Golgi intermediate compartment. Together with the co-receptor MCFD2, it transports coagulation factors V and VIII. Mutations in LMAN1 and MCFD2 can cause combined deficiency of factors V and VIII (F5F8D). We present the crystal structure of the LMAN1/MCFD2 complex and relate it to patient mutations. Circular dichroism data show that the majority of the substitution mutations give rise to a disordered or severely destabilized MCFD2 protein. The few stable mutation variants are found in the binding surface of the complex leading to impaired LMAN1 binding and F5F8D.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Protein ERGIC-53P49257Details
Multiple coagulation factor deficiency protein 2Q8NI22Details