1h3q: Difference between revisions

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<StructureSection load='1h3q' size='340' side='right'caption='[[1h3q]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1h3q' size='340' side='right'caption='[[1h3q]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1h3q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H3Q FirstGlance]. <br>
<table><tr><td colspan='2'>[[1h3q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H3Q FirstGlance]. <br>
</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=1h3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h3q OCA], [https://pdbe.org/1h3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h3q RCSB], [https://www.ebi.ac.uk/pdbsum/1h3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h3q ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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=1h3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h3q OCA], [https://pdbe.org/1h3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h3q RCSB], [https://www.ebi.ac.uk/pdbsum/1h3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h3q ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/TPPC2_MOUSE TPPC2_MOUSE]] Prevents ENO1-mediated transcriptional repression and antagonizes ENO1-mediated cell death. May play a role in vesicular transport from endoplasmic reticulum to Golgi (By similarity).  
[https://www.uniprot.org/uniprot/TPPC2_MOUSE TPPC2_MOUSE] Prevents ENO1-mediated transcriptional repression and antagonizes ENO1-mediated cell death. May play a role in vesicular transport from endoplasmic reticulum to Golgi (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h3q ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h3q ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
SEDL is an evolutionarily highly conserved protein in eukaryotic organisms. Deletions or point mutations in the SEDL gene are responsible for the genetic disease spondyloepiphyseal dysplasia tarda (SEDT), an X-linked skeletal disorder. SEDL has been identified as a component of the transport protein particle (TRAPP), critically involved in endoplasmic reticulum-to-Golgi vesicle transport. Herein, we report the 2.4 A resolution structure of SEDL, which reveals an unexpected similarity to the structures of the N-terminal regulatory domain of two SNAREs, Ykt6p and Sec22b, despite no sequence homology to these proteins. The similarity and the presence of unusually many solvent-exposed apolar residues of SEDL suggest that it serves regulatory and/or adaptor functions through multiple protein-protein interactions. Of the four known missense mutations responsible for SEDT, three mutations (S73L, F83S, V130D) map to the protein interior, where the mutations would disrupt the structure, and the fourth (D47Y) on a surface at which the mutation may abrogate functional interactions with a partner protein.
Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda.,Jang SB, Kim YG, Cho YS, Suh PG, Kim KH, Oh BH J Biol Chem. 2002 Dec 20;277(51):49863-9. Epub 2002 Oct 1. PMID:12361953<ref>PMID:12361953</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1h3q" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Cho, Y S]]
[[Category: Cho Y-S]]
[[Category: Jang, S B]]
[[Category: Jang SB]]
[[Category: Kim, Y G]]
[[Category: Kim Y-G]]
[[Category: Oh, B H]]
[[Category: Oh B-H]]
[[Category: Endoplasmic reticulum]]
[[Category: Golgi]]
[[Category: Sedl]]
[[Category: Sedt]]
[[Category: Transport]]
[[Category: Vesicle transport]]

Revision as of 14:27, 27 March 2024

Crystal structure of SEDL at 2.4 Angstroms resolutionCrystal structure of SEDL at 2.4 Angstroms resolution

Structural highlights

1h3q is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TPPC2_MOUSE Prevents ENO1-mediated transcriptional repression and antagonizes ENO1-mediated cell death. May play a role in vesicular transport from endoplasmic reticulum to Golgi (By similarity).

Evolutionary Conservation

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

1h3q, resolution 2.40Å

Drag the structure with the mouse to rotate

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OCA
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