Source:http://linkedlifedata.com/resource/pubmed/id/19143629
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 1
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pubmed:dateCreated |
2009-1-15
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pubmed:abstractText |
Alix [ALG-2 (apoptosis-linked gene 2)-interacting protein X] was originally identified as a protein that interacts with ALG-2, a member of the penta-EF-hand Ca(2+)-binding protein family. ALG-2 binds to its C-terminal proline-rich region that contains four tandem repeats of PXY (where X represents an uncharged amino acid). Recent X-ray crystal structural analyses of the Ca(2+)-free and Ca(2+)-bound forms of ALG-2, as well as the complex with an Alix oligopeptide, have revealed a mechanism of Ca(2+)-dependent binding of ALG-2 to its target protein. Binding of Ca(2+) to EF3 (third EF-hand) enables the side chain of Arg(125), present in the loop connecting EF3 and EF4 (fourth EF-hand), to move sufficiently to make a primary hydrophobic pocket accessible to the critical PPYP (Pro-Pro-Tyr-Pro) motif in Alix, which partially overlaps with the GPP (Gly-Pro-Pro) motif for binding to Cep55 (centrosome protein of 55 kDa). The fact that ALG-2 forms a homodimer and each monomer has one peptide-binding site indicates the possibility that ALG-2 bridges two interacting proteins, including Alix and Tsg101 (tumour susceptibility gene 101), and functions as a Ca(2+)-dependent adaptor protein.
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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/Apoptosis Regulatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PDCD6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1470-8752
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
190-4
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pubmed:meshHeading |
pubmed-meshheading:19143629-Apoptosis Regulatory Proteins,
pubmed-meshheading:19143629-Calcium,
pubmed-meshheading:19143629-Calcium-Binding Proteins,
pubmed-meshheading:19143629-Crystallography, X-Ray,
pubmed-meshheading:19143629-EF Hand Motifs,
pubmed-meshheading:19143629-Humans,
pubmed-meshheading:19143629-Peptides
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pubmed:year |
2009
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pubmed:articleTitle |
The mechanism of Ca2+-dependent recognition of Alix by ALG-2: insights from X-ray crystal structures.
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pubmed:affiliation |
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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