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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2008-4-8
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pubmed:abstractText |
Cyclic AMP serves as an intracellular messenger in cells and regulates a variety of biological functions by transmitting information through proteins. These proteins of different functions all consist of a cAMP-binding motif, and the structure of this motif is highly conserved with an exception of the loop 3 and 4. In current study, cAMP receptor protein was employed as a model system to investigate the function of the two loops. The results indicated that the loop 3 involves in the intersubunits communication of CRP, whereas the loop 4 involves in cAMP binding and interdomains communication.
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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 |
May
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pubmed:issn |
0141-8130
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
42
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
372-9
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pubmed:meshHeading |
pubmed-meshheading:18328555-Amino Acid Motifs,
pubmed-meshheading:18328555-Anisotropy,
pubmed-meshheading:18328555-Cyclic AMP,
pubmed-meshheading:18328555-Cyclic AMP Receptor Protein,
pubmed-meshheading:18328555-DNA,
pubmed-meshheading:18328555-Escherichia coli,
pubmed-meshheading:18328555-Ligands,
pubmed-meshheading:18328555-Microscopy, Fluorescence,
pubmed-meshheading:18328555-Models, Chemical,
pubmed-meshheading:18328555-Models, Molecular,
pubmed-meshheading:18328555-Molecular Conformation,
pubmed-meshheading:18328555-Protein Binding,
pubmed-meshheading:18328555-Protein Structure, Secondary,
pubmed-meshheading:18328555-Protein Structure, Tertiary,
pubmed-meshheading:18328555-Thermodynamics
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pubmed:year |
2008
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pubmed:articleTitle |
The role of loops 3 and 4 in the interdomains and intersubunits communication of E. coli cAMP receptor protein.
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pubmed:affiliation |
Department of Chemistry, Fudan University, Shanghai 200433, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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