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rdf:type |
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lifeskim:mentions |
umls-concept:C0021701,
umls-concept:C0063695,
umls-concept:C0439855,
umls-concept:C0678594,
umls-concept:C0851285,
umls-concept:C1514562,
umls-concept:C1704259,
umls-concept:C1705987,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2003941
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pubmed:issue |
1
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pubmed:dateCreated |
2003-1-15
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pubmed:abstractText |
The structure of the I domain of integrin alpha L beta 2 bound to the Ig superfamily ligand ICAM-1 reveals the open ligand binding conformation and the first example of an integrin-IgSF interface. The I domain Mg2+ directly coordinates Glu-34 of ICAM-1, and a dramatic swing of I domain residue Glu-241 enables a critical salt bridge. Liganded and unliganded structures for both high- and intermediate-affinity mutant I domains reveal that ligand binding can induce conformational change in the alpha L I domain and that allosteric signals can convert the closed conformation to intermediate or open conformations without ligand binding. Pulling down on the C-terminal alpha 7 helix with introduced disulfide bonds ratchets the beta 6-alpha 7 loop into three different positions in the closed, intermediate, and open conformations, with a progressive increase in affinity.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0092-8674
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pubmed:author |
pubmed-author:DongYichengY,
pubmed-author:JoachimiakAndrzejA,
pubmed-author:JunChang-DukCD,
pubmed-author:LiuJin-HuanJH,
pubmed-author:McCormackAlisonA,
pubmed-author:ShimaokaMotomuM,
pubmed-author:SpringerTimothy ATA,
pubmed-author:TakagiJunichiJ,
pubmed-author:WangJia-HuaiJH,
pubmed-author:XiaoTsanT,
pubmed-author:YangYutingY,
pubmed-author:ZhangRongguangR
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
112
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
99-111
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12526797-Amino Acid Substitution,
pubmed-meshheading:12526797-Animals,
pubmed-meshheading:12526797-Cells, Cultured,
pubmed-meshheading:12526797-Crystallography, X-Ray,
pubmed-meshheading:12526797-Disulfides,
pubmed-meshheading:12526797-Escherichia coli,
pubmed-meshheading:12526797-Glutamine,
pubmed-meshheading:12526797-Integrins,
pubmed-meshheading:12526797-Intercellular Adhesion Molecule-1,
pubmed-meshheading:12526797-Ligands,
pubmed-meshheading:12526797-Lymphocyte Function-Associated Antigen-1,
pubmed-meshheading:12526797-Magnesium,
pubmed-meshheading:12526797-Models, Molecular,
pubmed-meshheading:12526797-Molecular Conformation,
pubmed-meshheading:12526797-Mutation,
pubmed-meshheading:12526797-Protein Conformation,
pubmed-meshheading:12526797-Protein Structure, Secondary,
pubmed-meshheading:12526797-Protein Structure, Tertiary,
pubmed-meshheading:12526797-Spectrum Analysis, Raman,
pubmed-meshheading:12526797-Surface Plasmon Resonance
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pubmed:year |
2003
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pubmed:articleTitle |
Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation.
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pubmed:affiliation |
The Center for Blood Research, Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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