3LCP

Crystal structure of the carbohydrate recognition domain of LMAN1 in complex with MCFD2

Summary for 3LCP

• Entry DOI: 10.2210/pdb3lcp/pdb
• Descriptor: Protein ERGIC-53, Multiple coagulation factor deficiency protein 2, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: er-golgi transport, glycoprotein sorting, disease mutation, secretory pathway, protein transport, coagulation factor deficiency, disulfide bond, endoplasmic reticulum, golgi apparatus, lectin, membrane, polymorphism, transmembrane, transport, calcium, protein binding
• Biological source: Homo sapiens (human); More
• Cellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein: P49257; Endoplasmic reticulum-Golgi intermediate compartment: Q8NI22
• Total number of polymer chains: 4
• Total formula weight: 75511.93

Authors

Wigren, E.,Bourhis, J.M.,Kursula, I.,Guy, J.E.,Lindqvist, Y. (deposition date: 2010-01-11, release date: 2010-01-26, Last modification date: 2024-11-06)

Primary citation

Wigren, E.,Bourhis, J.M.,Kursula, I.,Guy, J.E.,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., 584:878-882, 2010

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.

PubMed: 20138881
DOI: 10.1016/j.febslet.2010.02.009

Experimental method

X-RAY DIFFRACTION (2.45 Å)