Source:http://linkedlifedata.com/resource/pubmed/id/11477072
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
39
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| pubmed:dateCreated |
2001-9-24
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| pubmed:abstractText |
In the primary sequence of the integrin beta subunit, the N-terminal region (NTR) and mid-region are separated by the I-like domain. To determine the spatial relationship and functional properties of the integrin beta(2) NTR and mid-region, we constructed beta(2)/beta(7) chimeras in which the NTR, I-like domain, and the mid-region of the beta(2) subunit were replaced by those of beta(7). Changing either the beta(2) NTR or mid-region, but not the I-like domain to that of beta(7) did not affect LFA-1 (alpha(L)beta(2)) formation and surface expression. Thus, the specificity of alpha(L)beta(2) pairing is conferred by the I-like domain but not the NTR or mid-region. Using these chimeras, the epitopes of six anti-beta(2) mAbs (H52, 7E4, AZN-L18, AZN-L27, KIM202, and MEM-148) were mapped. All except H52 require both the NTR and mid-region for epitope expression. Since these mAbs have distinct properties in terms of epitope expression and effect on LFA-1 binding to ICAM-1, we conclude that the beta(2) NTR and mid-region interact extensively. Although the I-like domain is located between the NTR and mid-region, its removal does not affect the folding of the beta(2) NTR/mid-region complex because this complex alone can be expressed as a soluble protein and precipitated by the appropriate mAbs. Finally, the mAbs H52 and 7E4, abrogated KIM185- but not Mg/EGTAinduced LFA-1/ICAM-1 binding and the epitope of MEM-148 is expressed on Mg/EGTA-activated but not resting LFA-1. These results suggest that the NTR/mid-region complex is involved in the regulation of LFA-1 function.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD18,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Adhesion Molecule-1,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphocyte Function-Associated...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Sep
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
28
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| pubmed:volume |
276
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
36370-6
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11477072-Amino Acid Sequence,
pubmed-meshheading:11477072-Animals,
pubmed-meshheading:11477072-Antibodies, Monoclonal,
pubmed-meshheading:11477072-Antigens, CD18,
pubmed-meshheading:11477072-COS Cells,
pubmed-meshheading:11477072-Cell Adhesion,
pubmed-meshheading:11477072-DNA, Complementary,
pubmed-meshheading:11477072-Epitopes,
pubmed-meshheading:11477072-Flow Cytometry,
pubmed-meshheading:11477072-Gene Library,
pubmed-meshheading:11477072-Humans,
pubmed-meshheading:11477072-Intercellular Adhesion Molecule-1,
pubmed-meshheading:11477072-Lymphocyte Function-Associated Antigen-1,
pubmed-meshheading:11477072-Molecular Sequence Data,
pubmed-meshheading:11477072-Precipitin Tests,
pubmed-meshheading:11477072-Protein Binding,
pubmed-meshheading:11477072-Protein Structure, Tertiary,
pubmed-meshheading:11477072-Transfection
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| pubmed:year |
2001
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| pubmed:articleTitle |
The N-terminal region and the mid-region complex of the integrin beta 2 subunit.
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| pubmed:affiliation |
Medical Research Council Immunochemistry Unit, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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