4cqo

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m (Protected "4cqo" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4cqo| PDB=4cqo | SCENE= }}
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===Structure of the human CNOT1 superfamily homology domain in complex with a Nanos1 peptide===
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The entry 4cqo is ON HOLD until Paper Publication
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==Disease==
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[[http://www.uniprot.org/uniprot/NANO1_HUMAN NANO1_HUMAN]] Male infertility due to NANOS1 mutation. The disease is caused by mutations affecting the gene represented in this entry.
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Authors: Raisch, T., Jonas, S., Weichenrieder, O., Bhandari, D., Izaurralde, E.
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==Function==
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[[http://www.uniprot.org/uniprot/CNOT1_HUMAN CNOT1_HUMAN]] Belongs to the CCR4-NOT complex that functions as general transcription regulation complex. Acts as a transcriptional repressor. Represses the ligand-dependent transcriptional activation by nuclear receptors.<ref>PMID:10637334</ref> <ref>PMID:16778766</ref> [[http://www.uniprot.org/uniprot/NANO1_HUMAN NANO1_HUMAN]] May act as a translational repressor which regulates translation of specific mRNAs by forming a complex with PUM2 that associates with the 3'-UTR of mRNA targets. Capable of interfering with the proadhesive and anti-invasive functions of E-cadherin. Up-regulates the production of MMP14 to promote tumor cell invasion.<ref>PMID:17047063</ref> <ref>PMID:18223680</ref>
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Description: Structure of the human CNOT1 superfamily homology domain in complex with a Nanos1 peptide
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==About this Structure==
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[[4cqo]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CQO OCA].
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Bhandari, D.]]
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[[Category: Izaurralde, E.]]
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[[Category: Jonas, S.]]
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[[Category: Raisch, T.]]
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[[Category: Weichenrieder, O.]]
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[[Category: Deadenylation]]
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[[Category: Development]]
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[[Category: Gene regulation]]
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[[Category: Protein complex]]
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[[Category: Short linear motif]]
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[[Category: Translation]]
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[[Category: Translational repression]]

Revision as of 07:51, 23 April 2014

Template:STRUCTURE 4cqo

Contents

Structure of the human CNOT1 superfamily homology domain in complex with a Nanos1 peptide

Disease

[NANO1_HUMAN] Male infertility due to NANOS1 mutation. The disease is caused by mutations affecting the gene represented in this entry.

Function

[CNOT1_HUMAN] Belongs to the CCR4-NOT complex that functions as general transcription regulation complex. Acts as a transcriptional repressor. Represses the ligand-dependent transcriptional activation by nuclear receptors.[1] [2] [NANO1_HUMAN] May act as a translational repressor which regulates translation of specific mRNAs by forming a complex with PUM2 that associates with the 3'-UTR of mRNA targets. Capable of interfering with the proadhesive and anti-invasive functions of E-cadherin. Up-regulates the production of MMP14 to promote tumor cell invasion.[3] [4]

About this Structure

4cqo is a 4 chain structure. Full crystallographic information is available from OCA.

Reference

  1. ↑ Albert TK, Lemaire M, van Berkum NL, Gentz R, Collart MA, Timmers HT. Isolation and characterization of human orthologs of yeast CCR4-NOT complex subunits. Nucleic Acids Res. 2000 Feb 1;28(3):809-17. PMID:10637334
  2. ↑ Winkler GS, Mulder KW, Bardwell VJ, Kalkhoven E, Timmers HT. Human Ccr4-Not complex is a ligand-dependent repressor of nuclear receptor-mediated transcription. EMBO J. 2006 Jul 12;25(13):3089-99. Epub 2006 Jun 15. PMID:16778766 doi:7601194
  3. ↑ Strumane K, Bonnomet A, Stove C, Vandenbroucke R, Nawrocki-Raby B, Bruyneel E, Mareel M, Birembaut P, Berx G, van Roy F. E-cadherin regulates human Nanos1, which interacts with p120ctn and induces tumor cell migration and invasion. Cancer Res. 2006 Oct 15;66(20):10007-15. PMID:17047063 doi:http://dx.doi.org/10.1158/0008-5472.CAN-05-3096
  4. ↑ Bonnomet A, Polette M, Strumane K, Gilles C, Dalstein V, Kileztky C, Berx G, van Roy F, Birembaut P, Nawrocki-Raby B. The E-cadherin-repressed hNanos1 gene induces tumor cell invasion by upregulating MT1-MMP expression. Oncogene. 2008 Jun 12;27(26):3692-9. doi: 10.1038/sj.onc.1211035. Epub 2008 Jan, 28. PMID:18223680 doi:http://dx.doi.org/10.1038/sj.onc.1211035

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