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rdf:type |
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lifeskim:mentions |
umls-concept:C0037633,
umls-concept:C0183362,
umls-concept:C0205148,
umls-concept:C0205164,
umls-concept:C0300824,
umls-concept:C0678594,
umls-concept:C1314939,
umls-concept:C1382100,
umls-concept:C1423827,
umls-concept:C1514562,
umls-concept:C1704675,
umls-concept:C1707271,
umls-concept:C1707798,
umls-concept:C1880352,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
2
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pubmed:dateCreated |
2001-7-31
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pubmed:abstractText |
p47 is the major protein identified in complex with the cytosolic AAA ATPase p97. It functions as an essential cofactor of p97-regulated membrane fusion, which has been suggested to disassemble t-t-SNARE complexes and prepare them for further rounds of membrane fusion. Here, we report the high-resolution NMR structure of the C-terminal domain from p47. It comprises a UBX domain and a 13 residue long structured N-terminal extension. The UBX domain adopts a characteristic ubiquitin fold with a betabetaalphabetabetaalphabeta secondary structure arrangement. Three hydrophobic residues from the N-terminal extension pack closely against a cleft in the UBX domain. We also identify, for the first time, the p97 interaction surface using NMR chemical shift perturbation studies.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/DEAD-box RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/Ddx39b protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/p97 ATPase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0022-2836
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2001 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
311
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
255-63
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:11478859-Adenosine Triphosphatases,
pubmed-meshheading:11478859-Amino Acid Sequence,
pubmed-meshheading:11478859-Animals,
pubmed-meshheading:11478859-Binding Sites,
pubmed-meshheading:11478859-DEAD-box RNA Helicases,
pubmed-meshheading:11478859-Membrane Proteins,
pubmed-meshheading:11478859-Models, Molecular,
pubmed-meshheading:11478859-Molecular Sequence Data,
pubmed-meshheading:11478859-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:11478859-Nuclear Proteins,
pubmed-meshheading:11478859-Protein Structure, Secondary,
pubmed-meshheading:11478859-Protein Structure, Tertiary,
pubmed-meshheading:11478859-Rats,
pubmed-meshheading:11478859-SNARE Proteins,
pubmed-meshheading:11478859-Sequence Alignment,
pubmed-meshheading:11478859-Solutions,
pubmed-meshheading:11478859-Ubiquitins,
pubmed-meshheading:11478859-Vesicular Transport Proteins
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pubmed:year |
2001
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pubmed:articleTitle |
Solution structure and interaction surface of the C-terminal domain from p47: a major p97-cofactor involved in SNARE disassembly.
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pubmed:affiliation |
Department of Biological Sciences, Wolfson Laboratories, Imperial College of Science Technology and Medicine, London, South Kensington, SW7 2AY, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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