| pubmed-article:17548821 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17548821 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:17548821 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:17548821 | lifeskim:mentions | umls-concept:C0332255 | lld:lifeskim |
| pubmed-article:17548821 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17548821 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:17548821 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:17548821 | lifeskim:mentions | umls-concept:C2348205 | lld:lifeskim |
| pubmed-article:17548821 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:17548821 | pubmed:dateCreated | 2007-6-13 | lld:pubmed |
| pubmed-article:17548821 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17548821 | pubmed:abstractText | Reelin, a large secreted protein implicated in the cortical development of the mammalian brain, is composed of eight tandem concatenations of "reelin repeats" and binds to neuronal receptors belonging to the low-density lipoprotein receptor gene family. We found that both receptor-binding and subsequent Dab1 phosphorylation occur solely in the segment spanning the fifth and sixth reelin repeats (R5-6). Monomeric fragment exhibited a suboptimal level of signaling activity and artificial oligomerization resulted in a 10-fold increase in activity, indicating the critical importance of higher-order multimerization in physiological reelin. A 2.0-A crystal structure from the R5-6 fragment revealed not only a unique domain arrangement wherein two repeats were aligned side by side with the same orientation, but also the unexpected presence of bound Zn ions. Structure-guided alanine mutagenesis of R5-6 revealed that two Lys residues (Lys-2360 and Lys-2467) constitute a central binding site for the low-density lipoprotein receptor class A module in the receptor, indicating a strong similarity to the ligand recognition mode shared among the endocytic lipoprotein receptors. | lld:pubmed |
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| pubmed-article:17548821 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17548821 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17548821 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17548821 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17548821 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:17548821 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:17548821 | pubmed:author | pubmed-author:TakagiJunichi... | lld:pubmed |
| pubmed-article:17548821 | pubmed:author | pubmed-author:NogiTerukazuT | lld:pubmed |
| pubmed-article:17548821 | pubmed:author | pubmed-author:NakanoYoshimi... | lld:pubmed |
| pubmed-article:17548821 | pubmed:author | pubmed-author:HattoriMitsuh... | lld:pubmed |
| pubmed-article:17548821 | pubmed:author | pubmed-author:YasuiNorihisa... | lld:pubmed |
| pubmed-article:17548821 | pubmed:author | pubmed-author:KitaoTomoeT | lld:pubmed |
| pubmed-article:17548821 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17548821 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:17548821 | pubmed:volume | 104 | lld:pubmed |
| pubmed-article:17548821 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17548821 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17548821 | pubmed:pagination | 9988-93 | lld:pubmed |
| pubmed-article:17548821 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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