rdf:type |
|
lifeskim:mentions |
umls-concept:C0031715,
umls-concept:C0037791,
umls-concept:C0080093,
umls-concept:C0248868,
umls-concept:C1152805,
umls-concept:C1273518,
umls-concept:C1415299,
umls-concept:C1415300,
umls-concept:C1519249,
umls-concept:C1521761,
umls-concept:C1711351
|
pubmed:issue |
1-2
|
pubmed:dateCreated |
2002-7-30
|
pubmed:abstractText |
Calcium/calmodulin-dependent protein kinase type II (CaMKII) and NMDA-type glutamate receptor (NMDAR) are neuronal proteins involved in learning and memory. CaMKII binds to the NR2B subunit of NMDAR in more than one mode, a stable association involving a noncatalytic site on CaMKII and an enzyme-substrate mode of interaction by its catalytic site. The latter binding results in phosphorylation of serine-1303 on NR2B. We have investigated this binding by studying the kinetics of phosphorylation of synthetic peptides harboring nested sequences of the phosphorylation site motif. We find that residues 1292-1297 of NR2B enhance the affinity of the catalytic site-mediated binding of CaMKII to the minimal phosphorylation site motif, 1298-1308 of NR2B, as evident from measurements of K(m) values for phosphorylation. However, CaMKII shows decreased affinity towards the closely related NR2A subunit due to an -Ile-Asn- motif present as a natural insertion in the analogous sequence on NR2A.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0006-3002
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
29
|
pubmed:volume |
1598
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
40-5
|
pubmed:dateRevised |
2007-11-15
|
pubmed:meshHeading |
pubmed-meshheading:12147342-Amino Acid Sequence,
pubmed-meshheading:12147342-Animals,
pubmed-meshheading:12147342-Calcium-Calmodulin-Dependent Protein Kinase Type 2,
pubmed-meshheading:12147342-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:12147342-Kinetics,
pubmed-meshheading:12147342-Molecular Sequence Data,
pubmed-meshheading:12147342-Peptide Fragments,
pubmed-meshheading:12147342-Phosphorylation,
pubmed-meshheading:12147342-Prosencephalon,
pubmed-meshheading:12147342-Protein Subunits,
pubmed-meshheading:12147342-Rats,
pubmed-meshheading:12147342-Receptors, N-Methyl-D-Aspartate,
pubmed-meshheading:12147342-Sequence Alignment,
pubmed-meshheading:12147342-Sequence Homology, Amino Acid,
pubmed-meshheading:12147342-Substrate Specificity
|
pubmed:year |
2002
|
pubmed:articleTitle |
Sequence determinants on the NR2A and NR2B subunits of NMDA receptor responsible for specificity of phosphorylation by CaMKII.
|
pubmed:affiliation |
Rajiv Gandhi Centre for Biotechnology, Jagathy, Thiruvananthapuam, Kerala-695014, India.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|