| pubmed-article:10830169 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10830169 | lifeskim:mentions | umls-concept:C0027882 | lld:lifeskim |
| pubmed-article:10830169 | lifeskim:mentions | umls-concept:C0007577 | lld:lifeskim |
| pubmed-article:10830169 | lifeskim:mentions | umls-concept:C0084710 | lld:lifeskim |
| pubmed-article:10830169 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:10830169 | lifeskim:mentions | umls-concept:C1517880 | lld:lifeskim |
| pubmed-article:10830169 | lifeskim:mentions | umls-concept:C1413560 | lld:lifeskim |
| pubmed-article:10830169 | lifeskim:mentions | umls-concept:C1705535 | lld:lifeskim |
| pubmed-article:10830169 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:10830169 | lifeskim:mentions | umls-concept:C1709061 | lld:lifeskim |
| pubmed-article:10830169 | lifeskim:mentions | umls-concept:C0453984 | lld:lifeskim |
| pubmed-article:10830169 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10830169 | pubmed:dateCreated | 2000-6-16 | lld:pubmed |
| pubmed-article:10830169 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10830169 | pubmed:abstractText | We have determined the crystal structure of the ligand binding fragment of the neural cell adhesion molecule axonin-1/TAG-1 comprising the first four immunoglobulin (Ig) domains. The overall structure of axonin-1(Ig1-4) is U-shaped due to contacts between domains 1 and 4 and domains 2 and 3. In the crystals, these molecules are aligned in a string with adjacent molecules oriented in an anti-parallel fashion and their C termini perpendicular to the string. This arrangement suggests that cell adhesion by homophilic axonin-1 interaction occurs by the formation of a linear zipper-like array in which the axonin-1 molecules are alternately provided by the two apposed membranes. In accordance with this model, mutations in a loop critical for the formation of the zipper resulted in the loss of the homophilic binding capacity of axonin-1. | lld:pubmed |
| pubmed-article:10830169 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10830169 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10830169 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10830169 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10830169 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10830169 | pubmed:month | May | lld:pubmed |
| pubmed-article:10830169 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:10830169 | pubmed:author | pubmed-author:SondereggerPP | lld:pubmed |
| pubmed-article:10830169 | pubmed:author | pubmed-author:LeddyTT | lld:pubmed |
| pubmed-article:10830169 | pubmed:author | pubmed-author:WelteWW | lld:pubmed |
| pubmed-article:10830169 | pubmed:author | pubmed-author:DiederichsKK | lld:pubmed |
| pubmed-article:10830169 | pubmed:author | pubmed-author:ProbaKK | lld:pubmed |
| pubmed-article:10830169 | pubmed:author | pubmed-author:FreigangJJ | lld:pubmed |
| pubmed-article:10830169 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10830169 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:10830169 | pubmed:volume | 101 | lld:pubmed |
| pubmed-article:10830169 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10830169 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10830169 | pubmed:pagination | 425-33 | lld:pubmed |
| pubmed-article:10830169 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:10830169 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10830169 | pubmed:articleTitle | The crystal structure of the ligand binding module of axonin-1/TAG-1 suggests a zipper mechanism for neural cell adhesion. | lld:pubmed |
| pubmed-article:10830169 | pubmed:affiliation | Faculty of Biology, University of Konstanz, Germany. | lld:pubmed |
| pubmed-article:10830169 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10830169 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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