2cp6: Difference between revisions

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==Solution structure of the 2nd CAP-Gly domain in human CLIP-170/restin==
==Solution structure of the 2nd CAP-Gly domain in human CLIP-170/restin==
<StructureSection load='2cp6' size='340' side='right'caption='[[2cp6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2cp6' size='340' side='right'caption='[[2cp6]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2cp6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CP6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2cp6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CP6 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FB2383_D01 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cp6 OCA], [https://pdbe.org/2cp6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cp6 RCSB], [https://www.ebi.ac.uk/pdbsum/2cp6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cp6 ProSAT], [https://www.topsan.org/Proteins/RSGI/2cp6 TOPSAN]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cp6 OCA], [https://pdbe.org/2cp6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cp6 RCSB], [https://www.ebi.ac.uk/pdbsum/2cp6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cp6 ProSAT], [https://www.topsan.org/Proteins/RSGI/2cp6 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/REST_HUMAN REST_HUMAN]] Transcriptional repressor which binds neuron-restrictive silencer element (NRSE) and represses neuronal gene transcription in non-neuronal cells. Restricts the expression of neuronal genes by associating with two distinct corepressors, mSin3 and CoREST, which in turn recruit histone deacetylase to the promoters of REST-regulated genes. Mediates repression by recruiting the BHC complex at RE1/NRSE sites which acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier.<ref>PMID:7697725</ref> <ref>PMID:7871435</ref> <ref>PMID:8568247</ref> <ref>PMID:12399542</ref>
[https://www.uniprot.org/uniprot/CLIP1_HUMAN CLIP1_HUMAN] Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking.<ref>PMID:12433698</ref> <ref>PMID:17889670</ref> <ref>PMID:17563362</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Inoue, M]]
[[Category: Inoue M]]
[[Category: Kigawa, T]]
[[Category: Kigawa T]]
[[Category: Koshiba, S]]
[[Category: Koshiba S]]
[[Category: Structural genomic]]
[[Category: Saito K]]
[[Category: Saito, K]]
[[Category: Yokoyama S]]
[[Category: Yokoyama, S]]
[[Category: Cytoskeleton associated protein]]
[[Category: Microtubule binding]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Protein binding]]
[[Category: Restin]]
[[Category: Rsgi]]

Latest revision as of 14:28, 22 May 2024

Solution structure of the 2nd CAP-Gly domain in human CLIP-170/restinSolution structure of the 2nd CAP-Gly domain in human CLIP-170/restin

Structural highlights

2cp6 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

CLIP1_HUMAN Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Sahin U, Neumann F, Tureci O, Schmits R, Perez F, Pfreundschuh M. Hodgkin and Reed-Sternberg cell-associated autoantigen CLIP-170/restin is a marker for dendritic cells and is involved in the trafficking of macropinosomes to the cytoskeleton, supporting a function-based concept of Hodgkin and Reed-Sternberg cells. Blood. 2002 Dec 1;100(12):4139-45. PMID:12433698 doi:10.1182/blood.V100.12.4139
  2. ↑ Slep KC, Vale RD. Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1. Mol Cell. 2007 Sep 21;27(6):976-91. PMID:17889670 doi:10.1016/j.molcel.2007.07.023
  3. ↑ Mishima M, Maesaki R, Kasa M, Watanabe T, Fukata M, Kaibuchi K, Hakoshima T. Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition. Proc Natl Acad Sci U S A. 2007 Jun 19;104(25):10346-51. Epub 2007 Jun 11. PMID:17563362
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