2k3h: Difference between revisions

No edit summary
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:2k3h.jpg|left|200px]]


<!--
==Structural determinants for Ca2+ and PIP2 binding by the C2A domain of rabphilin-3A==
The line below this paragraph, containing "STRUCTURE_2k3h", creates the "Structure Box" on the page.
<StructureSection load='2k3h' size='340' side='right'caption='[[2k3h]]' 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'>[[2k3h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K3H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K3H 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
{{STRUCTURE_2k3h|  PDB=2k3h  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2k3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k3h OCA], [https://pdbe.org/2k3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k3h RCSB], [https://www.ebi.ac.uk/pdbsum/2k3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k3h ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RP3A_MOUSE RP3A_MOUSE] Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal.
== 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/k3/2k3h_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=2k3h ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rabphilin-3A is a neuronal C2 domain tandem containing protein involved in vesicle trafficking. Both its C2 domains (C2A and C2B) are able to bind phosphatidylinositol 4,5-bisphosphate, a key player in the neurotransmitter release process. The rabphilin-3A C2A domain has previously been shown to bind inositol-1,4,5-trisphosphate (IP3; phosphatidylinositol 4,5-bisphosphate headgroup) in a Ca2+-dependent manner with a relatively high affinity (50 microm) in the presence of saturating concentrations of Ca2+. Moreover, IP3 and Ca2+ binding to the C2A domain mutually enhance each other. Here we present the Ca2+-bound solution structure of the C2A domain. Structural comparison with the previously published Ca2+-free crystal structure revealed that Ca2+ binding induces a conformational change of Ca2+ binding loop 3 (CBL3). Our IP3 binding studies as well as our IP3-C2A docking model show the active involvement of CBL3 in IP3 binding, suggesting that the conformational change on CBL3 upon Ca2+ binding enables the interaction with IP3 and vice versa, in line with a target-activated messenger affinity mechanism. Our data provide detailed structural insight into the functional properties of the rabphilin-3A C2A domain and reveal for the first time the structural determinants of a target-activated messenger affinity mechanism.


===Structural determinants for Ca2+ and PIP2 binding by the C2A domain of rabphilin-3A===
Structural determinants for Ca2+ and phosphatidylinositol 4,5-bisphosphate binding by the C2A domain of rabphilin-3A.,Coudevylle N, Montaville P, Leonov A, Zweckstetter M, Becker S J Biol Chem. 2008 Dec 19;283(51):35918-28. Epub 2008 Oct 21. PMID:18945677<ref>PMID:18945677</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2k3h" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
2K3H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K3H OCA].
*[[Exophilin 3D structures|Exophilin 3D structures]]
*[[Rabphilin|Rabphilin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Becker S]]
[[Category: Becker, S.]]
[[Category: Coudevylle N]]
[[Category: Coudevylle, N.]]
[[Category: Leonov A]]
[[Category: Leonov, A.]]
[[Category: Montaville P]]
[[Category: Montaville, P.]]
[[Category: Zweckstetter M]]
[[Category: Zweckstetter, M.]]
[[Category: C2 domain]]
[[Category: Calcium]]
[[Category: Cell junction]]
[[Category: Metal-binding]]
[[Category: Phosphoprotein]]
[[Category: Pip2]]
[[Category: Protein transport]]
[[Category: Synapse]]
[[Category: Tama mechanism]]
[[Category: Transport]]
[[Category: Zinc]]
[[Category: Zinc-finger]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 22 10:35:41 2008''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA