Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2001-6-15
pubmed:abstractText
We have investigated the structure of the cell adhesion molecule L1 by electron microscopy. We were particularly interested in the conformation of the four N-terminal immunoglobulin domains, because x-ray diffraction showed that these domains are bent into a horseshoe shape in the related molecules hemolin and axonin-1. Surprisingly, rotary-shadowed specimens showed the molecules to be elongated, with no indication of the horseshoe shape. However, sedimentation data suggested that these domains of L1 were folded into a compact shape in solution; therefore, this prompted us to look at the molecules by an alternative technique, negative stain. The negative stain images showed a compact shape consistent with the expected horseshoe conformation. We speculate that in rotary shadowing the contact with the mica caused a distortion of the protein, weakening the bonds forming the horseshoe and permitting the molecule to extend. We have thus confirmed that the L1 molecule is primarily in the horseshoe conformation in solution, and we have visualized for the first time its opening into an extended conformation. Our study resolves conflicting interpretations from previous electron microscopy studies of L1.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-10328925, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-10469653, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-10645969, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-10662501, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-10767310, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-10830169, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-10854279, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-11196321, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-1311675, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-1377696, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-1404391, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-1705558, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-2045418, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-2387585, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-2491853, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-2627374, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-2627381, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-2805067, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-3049624, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-3136168, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-3709531, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-537064, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-6368220, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-6725397, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-7328116, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-7512353, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-7679097, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-7826641, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-8176743, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-8274278, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-8425542, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-8458865, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-8548820, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-8641271, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-8893017, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-8921253, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-8947027, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-8978825, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-8996796, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-9214388, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-9354804, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-9427628, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-9568396, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-9610803, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-9703515, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-9762433, http://linkedlifedata.com/resource/pubmed/commentcorrection/11408583-9852159
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1059-1524
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1765-73
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:11408583-Cell Adhesion, pubmed-meshheading:11408583-Cell Line, pubmed-meshheading:11408583-Centrifugation, pubmed-meshheading:11408583-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:11408583-Glycosylation, pubmed-meshheading:11408583-Humans, pubmed-meshheading:11408583-Immunoglobulins, pubmed-meshheading:11408583-Insect Proteins, pubmed-meshheading:11408583-Leukocyte L1 Antigen Complex, pubmed-meshheading:11408583-Membrane Glycoproteins, pubmed-meshheading:11408583-Microscopy, Electron, pubmed-meshheading:11408583-Neural Cell Adhesion Molecules, pubmed-meshheading:11408583-Protein Conformation, pubmed-meshheading:11408583-Protein Folding, pubmed-meshheading:11408583-Protein Structure, Tertiary, pubmed-meshheading:11408583-Proteins, pubmed-meshheading:11408583-Recombinant Proteins
pubmed:year
2001
pubmed:articleTitle
Cell adhesion molecule L1 in folded (horseshoe) and extended conformations.
More...