| pubmed-article:6415289 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6415289 | lifeskim:mentions | umls-concept:C0001465 | lld:lifeskim |
| pubmed-article:6415289 | lifeskim:mentions | umls-concept:C0031711 | lld:lifeskim |
| pubmed-article:6415289 | lifeskim:mentions | umls-concept:C0917785 | lld:lifeskim |
| pubmed-article:6415289 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:6415289 | lifeskim:mentions | umls-concept:C2611155 | lld:lifeskim |
| pubmed-article:6415289 | lifeskim:mentions | umls-concept:C1706498 | lld:lifeskim |
| pubmed-article:6415289 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:6415289 | pubmed:dateCreated | 1983-12-17 | lld:pubmed |
| pubmed-article:6415289 | pubmed:abstractText | The binding sites for the allosteric activator, AMP, to glycogen phosphorylase b are described in detail utilizing the more precise knowledge of the native structure obtained from crystallographic restrained least-squares refinement than has hitherto been available. Localized conformational changes are seen at the allosteric effector site that include shifts of between 1 and 2 A for residues Tyr75 and Arg309 and very small shifts for the region of residues 42 to 44 from the symmetry-related subunit. Kinetic studies demonstrate that NADH inhibits the AMP activation of glycogen phosphorylase b. Crystallographic binding studies at 3.5 A resolution show that NADH binds to the same sites on the enzyme as AMP, i.e. the allosteric effector site N, which is close to the subunit-subunit interface, and the nucleoside inhibitor site I, which is some 12 A from the catalytic site. The conformations of NADH at the two sites are different but both conformations are "folded" so that the nicotinamide ring is close (approx. 6 A) to the adenine ring. These conformations are compared with those suggested from solution studies and with the extended conformations observed in the single crystal structure of NAD+ and for NAD bound to dehydrogenases. Possible mechanisms for NADH inhibition of phosphorylase activation are discussed. | lld:pubmed |
| pubmed-article:6415289 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6415289 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6415289 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6415289 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6415289 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6415289 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6415289 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6415289 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6415289 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6415289 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:6415289 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:6415289 | pubmed:author | pubmed-author:WilsonK SKS | lld:pubmed |
| pubmed-article:6415289 | pubmed:author | pubmed-author:JohnsonL NLN | lld:pubmed |
| pubmed-article:6415289 | pubmed:author | pubmed-author:SturaE AEA | lld:pubmed |
| pubmed-article:6415289 | pubmed:author | pubmed-author:SansomM SMS | lld:pubmed |
| pubmed-article:6415289 | pubmed:author | pubmed-author:ZanottoAA | lld:pubmed |
| pubmed-article:6415289 | pubmed:author | pubmed-author:Van de... | lld:pubmed |
| pubmed-article:6415289 | pubmed:author | pubmed-author:StuartD IDI | lld:pubmed |
| pubmed-article:6415289 | pubmed:author | pubmed-author:BabuY SYS | lld:pubmed |
| pubmed-article:6415289 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6415289 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:6415289 | pubmed:volume | 170 | lld:pubmed |
| pubmed-article:6415289 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6415289 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6415289 | pubmed:pagination | 529-65 | lld:pubmed |
| pubmed-article:6415289 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:6415289 | pubmed:meshHeading | pubmed-meshheading:6415289-... | lld:pubmed |
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| pubmed-article:6415289 | pubmed:meshHeading | pubmed-meshheading:6415289-... | lld:pubmed |
| pubmed-article:6415289 | pubmed:meshHeading | pubmed-meshheading:6415289-... | lld:pubmed |
| pubmed-article:6415289 | pubmed:meshHeading | pubmed-meshheading:6415289-... | lld:pubmed |
| pubmed-article:6415289 | pubmed:meshHeading | pubmed-meshheading:6415289-... | lld:pubmed |
| pubmed-article:6415289 | pubmed:meshHeading | pubmed-meshheading:6415289-... | lld:pubmed |
| pubmed-article:6415289 | pubmed:meshHeading | pubmed-meshheading:6415289-... | lld:pubmed |
| pubmed-article:6415289 | pubmed:year | 1983 | lld:pubmed |
| pubmed-article:6415289 | pubmed:articleTitle | Comparison of AMP and NADH binding to glycogen phosphorylase b. | lld:pubmed |
| pubmed-article:6415289 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6415289 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:6415289 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6415289 | lld:pubmed |
