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2p8q

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(New page: 200px<br /><applet load="2p8q" size="350" color="white" frame="true" align="right" spinBox="true" caption="2p8q, resolution 2.35&Aring;" /> '''Crystal Structure of...)
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==Overview==
==Overview==
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The nuclear import of uridine-rich ribonucleoproteins (U snRNPs) is, mediated by the transport adaptor snurportin 1 (SNP1). Similar to importin, alpha, SNP1 uses an N-terminal importin beta binding (sIBB) domain to, recruit the receptor importin beta and gain access to the nucleus. In this, paper, we demonstrate the sIBB-domain has a bipartite nature, which, contains two distinct binding determinants for importin beta. The first, determinant spans residues 25-65, and includes the previously identified, alphaIBB-region of homology. The second binding determinant encompasses, residues 1-24 and resembles region 1011-1035 of the nucleoporin 153, (Nup153). The two binding determinants synergize within the sIBB-domain to, confer a low nanomolar binding affinity for importin beta, (Kd ~2nM) in an, interaction that, in vitro, is displaced by RanGppNHp. We propose that in, vivo the synergy of Nup153 and nuclear RanGTP promotes translocation of U, snRNPs into the nucleus.
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The nuclear import of uridine-rich ribonucleoproteins (U snRNPs) is mediated by the transport adaptor snurportin 1 (SNP1). Similar to importin alpha, SNP1 uses an N-terminal importin beta binding (sIBB) domain to recruit the receptor importin beta and gain access to the nucleus. In this paper, we demonstrate the sIBB-domain has a bipartite nature, which contains two distinct binding determinants for importin beta. The first determinant spans residues 25-65, and includes the previously identified alphaIBB-region of homology. The second binding determinant encompasses residues 1-24 and resembles region 1011-1035 of the nucleoporin 153 (Nup153). The two binding determinants synergize within the sIBB-domain to confer a low nanomolar binding affinity for importin beta, (Kd ~2nM) in an interaction that, in vitro, is displaced by RanGppNHp. We propose that in vivo the synergy of Nup153 and nuclear RanGTP promotes translocation of U snRNPs into the nucleus.
==About this Structure==
==About this Structure==
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[[Category: snurportin]]
[[Category: snurportin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 10:50:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:27:04 2008''

Revision as of 16:27, 21 February 2008


2p8q, resolution 2.35Å

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Crystal Structure of human Importin beta bound to the Snurportin1 IBB-domain

Overview

The nuclear import of uridine-rich ribonucleoproteins (U snRNPs) is mediated by the transport adaptor snurportin 1 (SNP1). Similar to importin alpha, SNP1 uses an N-terminal importin beta binding (sIBB) domain to recruit the receptor importin beta and gain access to the nucleus. In this paper, we demonstrate the sIBB-domain has a bipartite nature, which contains two distinct binding determinants for importin beta. The first determinant spans residues 25-65, and includes the previously identified alphaIBB-region of homology. The second binding determinant encompasses residues 1-24 and resembles region 1011-1035 of the nucleoporin 153 (Nup153). The two binding determinants synergize within the sIBB-domain to confer a low nanomolar binding affinity for importin beta, (Kd ~2nM) in an interaction that, in vitro, is displaced by RanGppNHp. We propose that in vivo the synergy of Nup153 and nuclear RanGTP promotes translocation of U snRNPs into the nucleus.

About this Structure

2P8Q is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Molecular basis for the recognition of snurportin 1 by importin beta., Mitrousis G, Olia AS, Walker-Kopp N, Cingolani G, J Biol Chem. 2008 Jan 9;. PMID:18187419

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