Source:http://linkedlifedata.com/resource/pubmed/id/21514389
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2011-5-25
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pubmed:databankReference | |
pubmed:abstractText |
The hemolymph of the fifth instar larvae of the silkworm Bombyx mori contains a group of homologous proteins with a molecular weight of approximately 30 kDa, termed B. mori low molecular weight lipoproteins (Bmlps), which account for about 5% of the total plasma proteins. These so-called "30 K proteins" have been reported to be involved in the innate immune response and transportation of lipid and/or sugar. To elucidate their molecular functions, we determined the crystal structure of a 30 K protein, Bmlp7, at 1.91Å. It has two distinct domains: an all-? N-terminal domain (NTD) and an all-? C-terminal domain (CTD) of the ?-trefoil fold. Comparative structural analysis indicates that Bmlp7 represents a new family, adding to the 14 families currently identified, of the ?-trefoil superfamily. Structural comparison and simulation suggest that the NTD has a putative lipid-binding cavity, whereas the CTD has a potential sugar-binding site. However, we were unable to detect the binding of either lipid or sugar. Therefore, further investigations are needed to characterize the molecular function of this protein.
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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 |
Jul
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pubmed:issn |
1095-8657
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2011 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:volume |
175
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
97-103
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pubmed:meshHeading |
pubmed-meshheading:21514389-Amino Acid Sequence,
pubmed-meshheading:21514389-Animals,
pubmed-meshheading:21514389-Bombyx,
pubmed-meshheading:21514389-Conserved Sequence,
pubmed-meshheading:21514389-Crystallography, X-Ray,
pubmed-meshheading:21514389-Hemolymph,
pubmed-meshheading:21514389-Insect Proteins,
pubmed-meshheading:21514389-Molecular Sequence Data,
pubmed-meshheading:21514389-Protein Structure, Secondary,
pubmed-meshheading:21514389-Protein Structure, Tertiary,
pubmed-meshheading:21514389-Sequence Alignment
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pubmed:year |
2011
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pubmed:articleTitle |
Crystal structure of the 30 K protein from the silkworm Bombyx mori reveals a new member of the ?-trefoil superfamily.
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pubmed:affiliation |
Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei Anhui 230027, People's Republic of China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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