Pub. Date : 2002 Mar 29
PMID : 11781328
8 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Cyclic AMP receptor protein (CRP) is a homodimeric protein, which is activated by cAMP binding to function as a transcriptional regulator of many genes in prokaryotes. | Cyclic AMP | C-reactive protein | Homo sapiens |
| 2 | Cyclic AMP receptor protein (CRP) is a homodimeric protein, which is activated by cAMP binding to function as a transcriptional regulator of many genes in prokaryotes. | Cyclic AMP | C-reactive protein | Homo sapiens |
| 3 | Until now, the actual number of cAMP molecules that can be bound by CRP in solution has been ambiguous. | Cyclic AMP | C-reactive protein | Homo sapiens |
| 4 | Altogether, the results not only established for the first time that CRP possesses two cyclic AMP-binding sites in each monomer, even in a solution without DNA, but also suggest that the syn-cAMP binding sites of the CRP dimer can be formed by an allosteric conformational change of the protein upon the binding of two anti-cAMPs at the N-terminal domain. | Cyclic AMP | C-reactive protein | Homo sapiens |
| 5 | Altogether, the results not only established for the first time that CRP possesses two cyclic AMP-binding sites in each monomer, even in a solution without DNA, but also suggest that the syn-cAMP binding sites of the CRP dimer can be formed by an allosteric conformational change of the protein upon the binding of two anti-cAMPs at the N-terminal domain. | Cyclic AMP | C-reactive protein | Homo sapiens |
| 6 | Altogether, the results not only established for the first time that CRP possesses two cyclic AMP-binding sites in each monomer, even in a solution without DNA, but also suggest that the syn-cAMP binding sites of the CRP dimer can be formed by an allosteric conformational change of the protein upon the binding of two anti-cAMPs at the N-terminal domain. | Cyclic AMP | C-reactive protein | Homo sapiens |
| 7 | Altogether, the results not only established for the first time that CRP possesses two cyclic AMP-binding sites in each monomer, even in a solution without DNA, but also suggest that the syn-cAMP binding sites of the CRP dimer can be formed by an allosteric conformational change of the protein upon the binding of two anti-cAMPs at the N-terminal domain. | Cyclic AMP | C-reactive protein | Homo sapiens |
| 8 | In addition, a residue-specific inspection of the spectral changes provides some new structural information about the cAMP-induced allosteric activation of CRP. | Cyclic AMP | C-reactive protein | Homo sapiens |