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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2005-10-5
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pubmed:databankReference |
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pubmed:abstractText |
Thrombospondins (THBSs) are secreted glycoproteins that have key roles in interactions between cells and the extracellular matrix. Here, we describe the 2.6-A-resolution crystal structure of the glycosylated signature domain of human THBS2, which includes three epidermal growth factor-like modules, 13 aspartate-rich repeats and a lectin-like module. These elements interact extensively to form three structural regions termed the stalk, wire and globe. The THBS2 signature domain is stabilized by these interactions and by a network of 30 bound Ca(2+) ions and 18 disulfide bonds. The structure suggests how genetic alterations of THBSs result in disease.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-10089316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-11583953,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-11590138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-11723011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-12189245,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-12691755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-12718556,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-12732502,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-15014436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-15456750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-15707899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-15772310,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-15880723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-2478219,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-2579080,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-7118943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-7525586,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-7798222,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-8406456,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16186819-8654563
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1545-9993
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
910-4
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pubmed:dateRevised |
2010-12-3
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pubmed:meshHeading |
pubmed-meshheading:16186819-Amino Acid Sequence,
pubmed-meshheading:16186819-Bone Diseases,
pubmed-meshheading:16186819-Calcium,
pubmed-meshheading:16186819-Crystallization,
pubmed-meshheading:16186819-Humans,
pubmed-meshheading:16186819-Joint Diseases,
pubmed-meshheading:16186819-Molecular Sequence Data,
pubmed-meshheading:16186819-Mutation,
pubmed-meshheading:16186819-Protein Structure, Tertiary,
pubmed-meshheading:16186819-Thrombospondins
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pubmed:year |
2005
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pubmed:articleTitle |
Structure of the calcium-rich signature domain of human thrombospondin-2.
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pubmed:affiliation |
Department of Medicine, 4285B Medical Sciences Center, University of Wisconsin-Madison, 1300 University Avenue, Madison, Wisconsin 53706, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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