Linked Life Data

10964573

Source:http://linkedlifedata.com/resource/pubmed/id/10964573

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-10-2
pubmed:databankReference
pubmed:abstractText
Importin-beta is a nuclear transport factor which mediates the nuclear import of various nuclear proteins. The N-terminal 1-449 residue fragment of mouse importin-beta (impbeta449) possesses the ability to bidirectionally translocate through the nuclear pore complex (NPC), and to bind RanGTP. The structure of the uncomplexed form of impbeta449 has been solved at a 2.6 A resolution by X-ray crystallography. It consists of ten copies of the tandemly arrayed HEAT repeat and exhibits conformational flexibility which is involved in protein-protein interaction for nuclear transport. The overall conformation of the HEAT repeats shows that a twisted motion produces a significantly varied superhelical architecture from the previously reported structure of RanGTP-bound importin-beta. These conformational changes appear to be the sum of small conformational changes throughout the polypeptide. Such a flexibility, which resides in the stacked HEAT repeats, is essential for interaction with RanGTP or with NPCs. Furthermore, it was found that impbeta449 has a structural similarity with another nuclear migrating protein, namely beta-catenin, which is composed of another type of helix-repeated structure of ARM repeat. Interestingly, the essential regions for NPC translocation for both importin-beta and beta-catenin are spatially well overlapped with one another. This strongly indicates the importance of helix stacking of the HEAT or ARM repeats for NPC-passage.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
302
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
251-64
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10964573-Amino Acid Sequence, pubmed-meshheading:10964573-Biological Transport, pubmed-meshheading:10964573-Cell Nucleus, pubmed-meshheading:10964573-Crystallography, X-Ray, pubmed-meshheading:10964573-Cytoskeletal Proteins, pubmed-meshheading:10964573-Karyopherins, pubmed-meshheading:10964573-Models, Molecular, pubmed-meshheading:10964573-Molecular Sequence Data, pubmed-meshheading:10964573-Motion, pubmed-meshheading:10964573-Nuclear Localization Signals, pubmed-meshheading:10964573-Nuclear Proteins, pubmed-meshheading:10964573-Peptide Fragments, pubmed-meshheading:10964573-Pliability, pubmed-meshheading:10964573-Protein Binding, pubmed-meshheading:10964573-Protein Structure, Secondary, pubmed-meshheading:10964573-Recombinant Fusion Proteins, pubmed-meshheading:10964573-Repetitive Sequences, Amino Acid, pubmed-meshheading:10964573-Sequence Alignment, pubmed-meshheading:10964573-Trans-Activators, pubmed-meshheading:10964573-beta Catenin
pubmed:year
2000
pubmed:articleTitle
The adoption of a twisted structure of importin-beta is essential for the protein-protein interaction required for nuclear transport.
pubmed:affiliation
Institute for Protein Research, Osaka University, 3-2 Yamada-oka, Osaka, Suita, 565-0871, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't