Source:http://linkedlifedata.com/resource/pubmed/id/14643651
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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0017968,
umls-concept:C0205145,
umls-concept:C0332281,
umls-concept:C0392747,
umls-concept:C0444626,
umls-concept:C0597357,
umls-concept:C1148580,
umls-concept:C1416645,
umls-concept:C1416874,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C1947906
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pubmed:issue |
5
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pubmed:dateCreated |
2003-12-3
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pubmed:databankReference | |
pubmed:abstractText |
p58/ERGIC-53 is a calcium-dependent animal lectin that acts as a cargo receptor, binding to a set of glycoproteins in the endoplasmic reticulum (ER) and transporting them to the Golgi complex. It is similar in structure to calcium-dependent leguminous lectins. We have determined the structure of the carbohydrate-recognition domain of p58/ERGIC-53 in its calcium-bound form. The structure reveals localized but large conformational changes in relation to the previously determined metal ion-free structure, mapping mostly to the ligand-binding site. It reveals the presence of two calcium ion-binding sites located 6A apart, one of which has no equivalent in the plant lectins. The second metal ion-binding site present in that class of lectins, binding Mn(2+), is absent from p58/ERGIC-53. The absence of a short loop in the ligand-binding site in this protein suggests that it has adapted to optimally bind the high-mannose Man(8)(GlcNAc)(2) glycan common to glycoproteins at the ER exit stage.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
334
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
845-51
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14643651-Binding Sites,
pubmed-meshheading:14643651-Calcium,
pubmed-meshheading:14643651-Carbohydrate Metabolism,
pubmed-meshheading:14643651-Crystallography, X-Ray,
pubmed-meshheading:14643651-Mannose-Binding Lectins,
pubmed-meshheading:14643651-Membrane Proteins,
pubmed-meshheading:14643651-Metals,
pubmed-meshheading:14643651-Models, Molecular,
pubmed-meshheading:14643651-Protein Conformation
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pubmed:year |
2003
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pubmed:articleTitle |
The crystal structure of the carbohydrate-recognition domain of the glycoprotein sorting receptor p58/ERGIC-53 reveals an unpredicted metal-binding site and conformational changes associated with calcium ion binding.
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pubmed:affiliation |
Molecular Structural Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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