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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1998-9-1
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pubmed:databankReference |
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pubmed:abstractText |
The betagamma-crystallins form a superfamily of eye lens proteins comprised of multiple Greek motifs that are symmetrically organized into domains and higher assemblies. In the betaB2-crystallin dimer each polypeptide folds into two similar domains that are related to monomeric gamma-crystallin by domain swapping. The crystal structure of the circularly permuted two-domain betaB2 polypeptide shows that permutation converts intermolecular domain pairing into intramolecular pairing. However, the dimeric permuted protein is, in fact, half a native tetramer. This result shows how the sequential order of domains in multi-domain proteins can affect quaternary domain assembly.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-1772634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-2234050,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-2397202,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-2456887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-3052280,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-7464942,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-7610480,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-7833801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-7849599,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-7925715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-8063735,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-8289268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-8347566,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-8580836,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-8605629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-8999933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-9083108,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-9204285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-9204286,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9655330-9302991
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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 |
Jun
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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 |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1280-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9655330-Animals,
pubmed-meshheading:9655330-Crystallins,
pubmed-meshheading:9655330-Crystallization,
pubmed-meshheading:9655330-Crystallography, X-Ray,
pubmed-meshheading:9655330-Dimerization,
pubmed-meshheading:9655330-Macromolecular Substances,
pubmed-meshheading:9655330-Models, Molecular,
pubmed-meshheading:9655330-Molecular Sequence Data,
pubmed-meshheading:9655330-Protein Folding,
pubmed-meshheading:9655330-Rats
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pubmed:year |
1998
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pubmed:articleTitle |
Circular permutation of betaB2-crystallin changes the hierarchy of domain assembly.
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pubmed:affiliation |
Birkbeck College, Department of Crystallography, London, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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