| pubmed-article:7857921 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7857921 | lifeskim:mentions | umls-concept:C0206454 | lld:lifeskim |
| pubmed-article:7857921 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:7857921 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:7857921 | lifeskim:mentions | umls-concept:C1323274 | lld:lifeskim |
| pubmed-article:7857921 | lifeskim:mentions | umls-concept:C0282534 | lld:lifeskim |
| pubmed-article:7857921 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:7857921 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:7857921 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:7857921 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:7857921 | lifeskim:mentions | umls-concept:C1881217 | lld:lifeskim |
| pubmed-article:7857921 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:7857921 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:7857921 | lifeskim:mentions | umls-concept:C0596455 | lld:lifeskim |
| pubmed-article:7857921 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:7857921 | pubmed:dateCreated | 1995-3-22 | lld:pubmed |
| pubmed-article:7857921 | pubmed:abstractText | To investigate the effects of metal ion binding to the alpha-PDGFR kinase insert domain, a PCR product representing amino acid residues 691-795 (104 amino acids) was bacterially expressed and purified. Secondary structure prediction and circular dichroism spectroscopy indicated this domain to be a mixed alpha + beta protein with a large coil/turn contribution. This 16 kDa, soluble, nonphosphorylated domain bound to 45Ca2+ and 65Zn2+ through a common shared site. Of the unlabeled divalent and trivalent metal ions tested, Ho3+ = Zn2+ > Ni2+ > Ca2+ = Mn2+ > Mg2+, Ba2+ in competing for 45Ca2+ binding to this domain. In the presence of Ca2+ ions, the conformation of the KI domain changed significantly, and this changed conformation was resistant to subtilisin proteolysis. However, in the presence of Zn2+ ions, the conformation of the KI domain changed only slightly. Nevertheless, Zn2+ ions were more effective in rendering the KI domain resistant to proteolysis as compared to that shown by Ca2+ ions. In vitro binding studies using purified baculovirus-expressed alpha-PDGFR showed a marked increase in binding the p85 N-SH2 domain in the presence of Ca2+ or Zn2+ ions (KD = 0.5 microM), suggesting that metal ion binding enhances association of the p85 N-SH2 domain with the receptor. To confirm this, association of the alpha-PDGFR with the p85 N-SH2 domain was tested in the presence of the KI domain. The nonphosphorylated KI domain was effective in competing with the alpha-PDGFR for the binding of the p85 N-SH2 domain. This effect was more pronounced in the presence of Ca2+ ions. Microinjection of this domain into Xenopus oocytes delayed maturation in the presence of insulin but not progesterone. This suggests that the KI domain has a correctly folded three-dimensional structure compatible with biological activity. Together these findings indicate that the recombinant alpha-PDGFR KI domain binds the p85 N-SH2 domain and this binding is modulated by the presence of a novel divalent metal ion binding site within its structure. | lld:pubmed |
| pubmed-article:7857921 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7857921 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7857921 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7857921 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7857921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7857921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7857921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7857921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7857921 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7857921 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:7857921 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:7857921 | pubmed:author | pubmed-author:McPhiePP | lld:pubmed |
| pubmed-article:7857921 | pubmed:author | pubmed-author:SantosEE | lld:pubmed |
| pubmed-article:7857921 | pubmed:author | pubmed-author:WlodawerAA | lld:pubmed |
| pubmed-article:7857921 | pubmed:author | pubmed-author:YuJ CJC | lld:pubmed |
| pubmed-article:7857921 | pubmed:author | pubmed-author:ThankiNN | lld:pubmed |
| pubmed-article:7857921 | pubmed:author | pubmed-author:HeidaranM AMA | lld:pubmed |
| pubmed-article:7857921 | pubmed:author | pubmed-author:ArocaPP | lld:pubmed |
| pubmed-article:7857921 | pubmed:author | pubmed-author:MahadevanDD | lld:pubmed |
| pubmed-article:7857921 | pubmed:author | pubmed-author:BeelerJJ | lld:pubmed |
| pubmed-article:7857921 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7857921 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:7857921 | pubmed:volume | 34 | lld:pubmed |
| pubmed-article:7857921 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7857921 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7857921 | pubmed:pagination | 2095-106 | lld:pubmed |
| pubmed-article:7857921 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:7857921 | pubmed:meshHeading | pubmed-meshheading:7857921-... | lld:pubmed |
| pubmed-article:7857921 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7857921 | pubmed:articleTitle | A divalent metal ion binding site in the kinase insert domain of the alpha-platelet-derived growth factor receptor regulates its association with SH2 domains. | lld:pubmed |
| pubmed-article:7857921 | pubmed:affiliation | Laboratory of Cellular and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892. | lld:pubmed |
| pubmed-article:7857921 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7857921 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:7857921 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:7857921 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7857921 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7857921 | lld:pubmed |
