3lcp
From Proteopedia
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{{STRUCTURE_3lcp| PDB=3lcp | SCENE= }} | {{STRUCTURE_3lcp| PDB=3lcp | SCENE= }} | ||
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===Crystal structure of the carbohydrate recognition domain of LMAN1 in complex with MCFD2=== | ===Crystal structure of the carbohydrate recognition domain of LMAN1 in complex with MCFD2=== | ||
| + | {{ABSTRACT_PUBMED_20138881}} | ||
| + | ==Disease== | ||
| + | [[http://www.uniprot.org/uniprot/LMAN1_HUMAN LMAN1_HUMAN]] Defects in LMAN1 are THE cause of factor V and factor VIII combined deficiency type 1 (F5F8D1) [MIM:[http://omim.org/entry/227300 227300]]; also known as multiple coagulation factor deficiency I (MCFD1). F5F8D1 is an autosomal recessive blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.<ref>PMID:10090935</ref> [[http://www.uniprot.org/uniprot/MCFD2_HUMAN MCFD2_HUMAN]] Defects in MCFD2 are a cause of factor V and factor VIII combined deficiency type 2 (F5F8D2) [MIM:[http://omim.org/entry/613625 613625]]; also known as multiple coagulation factor deficiency 2 (MCFD2). F5F8D2 is a blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.<ref>PMID:12717434</ref><ref>PMID:18590741</ref> | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/LMAN1_HUMAN LMAN1_HUMAN]] Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins.<ref>PMID:13130098</ref><ref>PMID:12717434</ref> [[http://www.uniprot.org/uniprot/MCFD2_HUMAN MCFD2_HUMAN]] The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. Plays a role in the secretion of coagulation factors.<ref>PMID:12717434</ref> | |
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==About this Structure== | ==About this Structure== | ||
| - | + | [[3lcp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LCP OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020138881</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Bourhis, J M.]] | [[Category: Bourhis, J M.]] | ||
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[[Category: Lindqvist, Y.]] | [[Category: Lindqvist, Y.]] | ||
[[Category: Wigren, E.]] | [[Category: Wigren, E.]] | ||
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[[Category: Coagulation factor deficiency]] | [[Category: Coagulation factor deficiency]] | ||
[[Category: Disease mutation]] | [[Category: Disease mutation]] | ||
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[[Category: Lectin]] | [[Category: Lectin]] | ||
[[Category: Membrane]] | [[Category: Membrane]] | ||
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[[Category: Protein binding]] | [[Category: Protein binding]] | ||
[[Category: Protein transport]] | [[Category: Protein transport]] | ||
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[[Category: Transmembrane]] | [[Category: Transmembrane]] | ||
[[Category: Transport]] | [[Category: Transport]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 28 10:52:53 2010'' | ||
Revision as of 19:43, 24 March 2013
Contents |
Crystal structure of the carbohydrate recognition domain of LMAN1 in complex with MCFD2
Template:ABSTRACT PUBMED 20138881
Disease
[LMAN1_HUMAN] Defects in LMAN1 are THE cause of factor V and factor VIII combined deficiency type 1 (F5F8D1) [MIM:227300]; also known as multiple coagulation factor deficiency I (MCFD1). F5F8D1 is an autosomal recessive blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.[1] [MCFD2_HUMAN] Defects in MCFD2 are a cause of factor V and factor VIII combined deficiency type 2 (F5F8D2) [MIM:613625]; also known as multiple coagulation factor deficiency 2 (MCFD2). F5F8D2 is a blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.[2][3]
Function
[LMAN1_HUMAN] Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins.[4][5] [MCFD2_HUMAN] The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. Plays a role in the secretion of coagulation factors.[6]
About this Structure
3lcp is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- 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. Epub 2010 Feb 9. PMID:20138881 doi:10.1016/j.febslet.2010.02.009
- ↑ Nichols WC, Terry VH, Wheatley MA, Yang A, Zivelin A, Ciavarella N, Stefanile C, Matsushita T, Saito H, de Bosch NB, Ruiz-Saez A, Torres A, Thompson AR, Feinstein DI, White GC, Negrier C, Vinciguerra C, Aktan M, Kaufman RJ, Ginsburg D, Seligsohn U. ERGIC-53 gene structure and mutation analysis in 19 combined factors V and VIII deficiency families. Blood. 1999 Apr 1;93(7):2261-6. PMID:10090935
- ↑ Zhang B, Cunningham MA, Nichols WC, Bernat JA, Seligsohn U, Pipe SW, McVey JH, Schulte-Overberg U, de Bosch NB, Ruiz-Saez A, White GC, Tuddenham EG, Kaufman RJ, Ginsburg D. Bleeding due to disruption of a cargo-specific ER-to-Golgi transport complex. Nat Genet. 2003 Jun;34(2):220-5. PMID:12717434 doi:10.1038/ng1153
- ↑ Guy JE, Wigren E, Svard M, Hard T, Lindqvist Y. New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2. J Mol Biol. 2008 Sep 12;381(4):941-55. Epub 2008 Jun 20. PMID:18590741 doi:10.1016/j.jmb.2008.06.042
- ↑ Nufer O, Kappeler F, Guldbrandsen S, Hauri HP. ER export of ERGIC-53 is controlled by cooperation of targeting determinants in all three of its domains. J Cell Sci. 2003 Nov 1;116(Pt 21):4429-40. Epub 2003 Sep 16. PMID:13130098 doi:10.1242/jcs.00759
- ↑ Zhang B, Cunningham MA, Nichols WC, Bernat JA, Seligsohn U, Pipe SW, McVey JH, Schulte-Overberg U, de Bosch NB, Ruiz-Saez A, White GC, Tuddenham EG, Kaufman RJ, Ginsburg D. Bleeding due to disruption of a cargo-specific ER-to-Golgi transport complex. Nat Genet. 2003 Jun;34(2):220-5. PMID:12717434 doi:10.1038/ng1153
- ↑ Zhang B, Cunningham MA, Nichols WC, Bernat JA, Seligsohn U, Pipe SW, McVey JH, Schulte-Overberg U, de Bosch NB, Ruiz-Saez A, White GC, Tuddenham EG, Kaufman RJ, Ginsburg D. Bleeding due to disruption of a cargo-specific ER-to-Golgi transport complex. Nat Genet. 2003 Jun;34(2):220-5. PMID:12717434 doi:10.1038/ng1153
Categories: Homo sapiens | Bourhis, J M. | Guy, J E. | Kursula, I. | Lindqvist, Y. | Wigren, E. | Coagulation factor deficiency | Disease mutation | Disulfide bond | Endoplasmic reticulum | Er-golgi transport | Glycoprotein sorting | Golgi apparatus | Lectin | Membrane | Protein binding | Protein transport | Secretory pathway | Transmembrane | Transport
