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Article

Structural characterization of carbohydrate binding by LMAN1 protein provides new insight into the endoplasmic reticulum export of factors V (FV) and VIII (FVIII).

The Journal of biological chemistry - 12 Jul 2013

Zheng Chunlei, Page Richard C, Das Vaijayanti, Nix Jay C, Wigren Edvard, Misra Saurav, Zhang Bin

Abstract excerpt

LMAN1 (ERGIC-53) is a key mammalian cargo receptor responsible for the export of a subset of glycoproteins from the endoplasmic reticulum. Together with its soluble coreceptor MCFD2, LMAN1 transports coagulation factors V (FV) and VIII (FVIII). Mutations in LMAN1 or MCFD2 cause the genetic bleeding disorder combined deficiency of FV and FVIII (F5F8D). The LMAN1 carbohydrate recognition domain (CRD) binds to both...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Open in PubMed Open full text

Identifiers

PMID: 23709226
DOI: 10.1074/jbc.M113.461434
PMCID: PMC3711315

Genes

LMAN1
MCFD2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Structural characterization of carbohydrate binding by LMAN1 protein provides new insight into the endoplasmic reticulum export of factors V (FV) and VIII (FVIII).PMID 23709226Read ↗

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Combined deficiency of coagulation factors V and VIII: an update.Semantic proximity Read ↗

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

Bleeding due to disruption of a cargo-specific ER-to-Golgi transport complex.Semantic proximity Read ↗

Factor VIII C1 domain spikes 2092-2093 and 2158-2159 comprise regions that modulate cofactor function and cellular uptake.Semantic proximity Read ↗

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Combined deficiency of factor V and factor VIII is due to mutations in either LMAN1 or MCFD2.Semantic proximity Read ↗

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