4e4v

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'''Unreleased structure'''
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{{STRUCTURE_4e4v| PDB=4e4v | SCENE= }}
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===The crystal structure of the dimeric human importin alpha 1 at 2.5 angstrom resolution.===
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The entry 4e4v is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/IMA2_HUMAN IMA2_HUMAN]] Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
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Authors: Hang, P.C., Miknis, Z.M., Franke, W.A., Umland, T.C., Schultz, L.W.
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==About this Structure==
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[[4e4v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E4V OCA].
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Description: The crystal structure of the dimeric human importin alpha 1 at 2.5 angstrom resolution.
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[[Category: Homo sapiens]]
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[[Category: Franke, W A.]]
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[[Category: Hang, P C.]]
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[[Category: Miknis, Z M.]]
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[[Category: Schultz, L W.]]
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[[Category: Umland, T C.]]
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[[Category: Armadillo repeat]]
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[[Category: Host-virus interaction]]
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[[Category: Importin]]
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[[Category: Karyopherin]]
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[[Category: Nuclear import]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Protein transport]]
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[[Category: Transport]]
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[[Category: Transport protein]]

Revision as of 16:17, 19 June 2013

Template:STRUCTURE 4e4v

The crystal structure of the dimeric human importin alpha 1 at 2.5 angstrom resolution.

Function

[IMA2_HUMAN] Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.

About this Structure

4e4v is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

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