2kiv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:47, 9 May 2024) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2kiv.png|left|200px]]
 
-
<!--
+
==AIDA-1 SAM domain tandem==
-
The line below this paragraph, containing "STRUCTURE_2kiv", creates the "Structure Box" on the page.
+
<StructureSection load='2kiv' size='340' side='right'caption='[[2kiv]]' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2kiv]] 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=2KIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KIV FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</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=2kiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kiv OCA], [https://pdbe.org/2kiv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kiv RCSB], [https://www.ebi.ac.uk/pdbsum/2kiv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kiv ProSAT]</span></td></tr>
-
{{STRUCTURE_2kiv| PDB=2kiv | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ANS1B_HUMAN ANS1B_HUMAN] Isoform 2 may participate in the regulation of nucleoplasmic coilin protein interactions in neuronal and transformed cells.<ref>PMID:15862129</ref> <ref>PMID:15347684</ref> Isoform 3 can regulate global protein synthesis by altering nucleolar numbers (By similarity).<ref>PMID:15862129</ref> <ref>PMID:15347684</ref> Isoform 4 may play a role as a modulator of APP processing. Overexpression can down-regulate APP processing.<ref>PMID:15862129</ref> <ref>PMID:15347684</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ki/2kiv_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=2kiv ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The neuronal scaffolding protein AIDA-1 is believed to act as a convener of signals arising at postsynaptic densities. Among the readily identifiable domains in AIDA-1, two closely juxtaposed sterile alpha motif (SAM) domains and a phosphotyrosine binding domain are located within the C-terminus of the longest splice variant and exclusively in four shorter splice variants. As a first step towards understanding the possible emergent properties arising from this assembly of ligand binding domains, we have used NMR methods to solve the first structure of a SAM domain tandem. Separated by a 15-aa linker, the two SAM domains are fused in a head-to-tail orientation that has been observed in other hetero- and homotypic SAM domain structures. The basic nuclear import signal for AIDA-1 is buried at the interface between the two SAM domains. An observed disparity between the thermal stabilities of the two SAM domains suggests a mechanism whereby the second SAM domain decouples from the first SAM domain to facilitate translocation of AIDA-1 to the nucleus.
-
===AIDA-1 SAM domain tandem===
+
A nuclear localization signal at the SAM-SAM domain interface of AIDA-1 suggests a requirement for domain uncoupling prior to nuclear import.,Kurabi A, Brener S, Mobli M, Kwan JJ, Donaldson LW J Mol Biol. 2009 Oct 9;392(5):1168-77. Epub 2009 Aug 8. PMID:19666031<ref>PMID:19666031</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
==About this Structure==
+
</div>
-
2KIV is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KIV OCA].
+
<div class="pdbe-citations 2kiv" style="background-color:#fffaf0;"></div>
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:19666031</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Donaldson, L W.]]
+
[[Category: Large Structures]]
-
[[Category: Kurabi, A.]]
+
[[Category: Donaldson LW]]
-
[[Category: Alternative splicing]]
+
[[Category: Kurabi A]]
-
[[Category: Ank repeat]]
+
-
[[Category: Cell junction]]
+
-
[[Category: Cell membrane]]
+
-
[[Category: Cell projection]]
+
-
[[Category: Cytoplasm]]
+
-
[[Category: Membrane]]
+
-
[[Category: Nucleus]]
+
-
[[Category: Phosphoprotein]]
+
-
[[Category: Postsynaptic cell membrane]]
+
-
[[Category: Sam domain]]
+
-
[[Category: Signaling protein]]
+
-
[[Category: Synapse]]
+
-
[[Category: Tandem]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Sep 21 16:36:36 2009''
+

Current revision

AIDA-1 SAM domain tandem

PDB ID 2kiv

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2kiv"
Personal tools