| pubmed-article:7889931 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7889931 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:7889931 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:7889931 | lifeskim:mentions | umls-concept:C1155872 | lld:lifeskim |
| pubmed-article:7889931 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:7889931 | pubmed:dateCreated | 1995-4-20 | lld:pubmed |
| pubmed-article:7889931 | pubmed:abstractText | p13suc1 binds to p34cdc2 kinase and is essential for cell cycle progression in eukaryotic cells. The crystal structure of S.pombe p13suc1 has been solved to 2.7 A resolution using data collected at the ESRF source, Grenoble, from both native crystals and crystals of a seleno-methionine derivative. The starting point for structure solution was the determination of the six selenium sites by direct methods. The structure is dominated by a four-stranded beta-sheet, with four further alpha-helical regions. p13suc1 crystallizes as a dimer in the asymmetric unit stabilized by the binding of two zinc ions. A third zinc site stabilizes the higher-order crystal packing. The sites are consistent with a requirement for zinc during crystal growth. A likely site for p13suc1-protein interaction is immediately evident on one face of the p13suc1 surface. This region comprises a group of conserved, exposed aromatic and hydrophobic residues below a flexible negatively charged loop. A conserved positively charged area would also present a notable surface feature in the monomer, but is buried at the dimer interface. p13suc1 is larger than its recently solved human homologue p9CKS2, with the extra polypeptide forming a helical N-terminal extension and a surface loop between alpha-helices 3 and 4. Notably, p13suc1 does not show the unusual beta-strand exchange that creates an intimate p9CKS2 dimer. p13suc1 cannot oligomerize to form a stable hexamer as has been proposed for p9CKS2. | lld:pubmed |
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| pubmed-article:7889931 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7889931 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7889931 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7889931 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7889931 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:7889931 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:7889931 | pubmed:author | pubmed-author:RasmussenBB | lld:pubmed |
| pubmed-article:7889931 | pubmed:author | pubmed-author:BrownNN | lld:pubmed |
| pubmed-article:7889931 | pubmed:author | pubmed-author:JohnsonL NLN | lld:pubmed |
| pubmed-article:7889931 | pubmed:author | pubmed-author:NursePP | lld:pubmed |
| pubmed-article:7889931 | pubmed:author | pubmed-author:NobleM EME | lld:pubmed |
| pubmed-article:7889931 | pubmed:author | pubmed-author:EndicottJ AJA | lld:pubmed |
| pubmed-article:7889931 | pubmed:author | pubmed-author:GarmanE FEF | lld:pubmed |
| pubmed-article:7889931 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7889931 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7889931 | pubmed:volume | 14 | lld:pubmed |
