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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1990-12-18
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pubmed:abstractText |
The crystal structure of oncomodulin, a 12,000 Mr protein isolated from rat tumours, has been determined by molecular replacement using the carp parvalbumin structure as a starting model. Refinement was performed by cycles of molecular fitting and restrained least-squares, using area-detector intensity data to 1.85 A resolution. For the 5770 reflections in the range 6.0 to 1.85 A, which were used in the refinement, the crystallographic R-factor is 0.166. The refined model includes residues 2 to 108, three Ca2+ and 87 water molecules per oncomodulin molecule. The oncomodulin backbone is closely related to that of parvalbumin; however, some differences are found after a least-squares fit of the two backbones, with root-mean-square (r.m.s.) deviations of 1 to 2 A in residues 2 to 6, 59 to 61 of the CD loop, 87, 90 and 108. The overall r.m.s. deviation of the backbone residues 5 to 108 is 0.62 A. Each of the two Ca2+ atoms that are bound to the CD and EF loops is co-ordinated to seven oxygen atoms, including one water molecule. The third Ca2+ is also seven-co-ordinated, to five oxygen atoms belonging to three different oncomodulin molecules and to two water molecules which form hydrogen bonds to a fourth oncomodulin; thus, this intermolecular Ca2+ and its equivalents interlink the molecules into zigzag layers normal to the b axis with a spacing of b/2 or 32.14 A. No such extensive molecular aggregation has been reported for any of the related Ca-binding regulatory proteins of the troponin-C family studied thus far. The Ca-O distances in all three polyhedra are in the range 2.07 A to 2.64 A, indicating tightly bound Ca polyhedra.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Parvalbumins,
http://linkedlifedata.com/resource/pubmed/chemical/oncomodulin
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
216
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
127-40
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2231727-Amino Acid Sequence,
pubmed-meshheading:2231727-Animals,
pubmed-meshheading:2231727-Calcium,
pubmed-meshheading:2231727-Calcium-Binding Proteins,
pubmed-meshheading:2231727-Computer Graphics,
pubmed-meshheading:2231727-Macromolecular Substances,
pubmed-meshheading:2231727-Models, Molecular,
pubmed-meshheading:2231727-Molecular Sequence Data,
pubmed-meshheading:2231727-Neoplasm Proteins,
pubmed-meshheading:2231727-Parvalbumins,
pubmed-meshheading:2231727-Protein Conformation,
pubmed-meshheading:2231727-Rats,
pubmed-meshheading:2231727-Sequence Homology, Nucleic Acid,
pubmed-meshheading:2231727-X-Ray Diffraction
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pubmed:year |
1990
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pubmed:articleTitle |
Structure of oncomodulin refined at 1.85 A resolution. An example of extensive molecular aggregation via Ca2+.
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pubmed:affiliation |
Division of Biological Sciences, National Research Council of Canada, Ottawa.
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pubmed:publicationType |
Journal Article,
Comparative Study
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