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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1993-4-22
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pubmed:abstractText |
cDNA coding for N-terminally truncated human annexin I, a member of the family of Ca(2+)-dependent phospholipid binding proteins, has been cloned and expressed in Escherichia coli. The expressed protein is biologically active, and has been purified and crystallized in space group P2(1)2(1)2(1) with cell dimensions a = 139.36 A, b = 67.50 A, and c = 42.11 A. The crystal structure has been determined by molecular replacement at 3.0 A resolution using the annexin V core structure as the search model. The average backbone deviation between these two structures is 2.34 A. The structure has been refined to an R-factor of 17.7% at 2.5 A resolution. Six calcium sites have been identified in the annexin I structure. Each is located in the loop region of the helix-loop-helix motif. Two of the six calcium sites in annexin I are not occupied in the annexin V structure. The superpositions of the corresponding loop regions in the four domains show that the calcium binding loops in annexin I can be divided into two classes: type II and type III. Both classes are different from the well-known EF-hand motif (type I).
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-1237625,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-1707872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-1830342,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-1864864,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-2137999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-2144646,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-2147412,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-2148156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-2206482,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-2454134,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-2540167,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-2936963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-2952659,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-2971450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-2973805,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-3032981,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8453382-7356955
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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 |
Mar
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
448-58
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8453382-Amino Acid Sequence,
pubmed-meshheading:8453382-Annexin A1,
pubmed-meshheading:8453382-Annexin A5,
pubmed-meshheading:8453382-Binding Sites,
pubmed-meshheading:8453382-Calcium,
pubmed-meshheading:8453382-Cloning, Molecular,
pubmed-meshheading:8453382-Escherichia coli,
pubmed-meshheading:8453382-Humans,
pubmed-meshheading:8453382-Models, Molecular,
pubmed-meshheading:8453382-Molecular Sequence Data,
pubmed-meshheading:8453382-Molecular Structure,
pubmed-meshheading:8453382-Protein Conformation,
pubmed-meshheading:8453382-Protein Structure, Secondary,
pubmed-meshheading:8453382-Sequence Homology, Amino Acid,
pubmed-meshheading:8453382-X-Ray Diffraction
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pubmed:year |
1993
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pubmed:articleTitle |
Crystal structure of human annexin I at 2.5 A resolution.
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pubmed:affiliation |
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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