1vyh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:08, 13 December 2023) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1vyh.gif|left|200px]]
 
-
<!--
+
==PAF-AH Holoenzyme: Lis1/Alfa2==
-
The line below this paragraph, containing "STRUCTURE_1vyh", creates the "Structure Box" on the page.
+
<StructureSection load='1vyh' size='340' side='right'caption='[[1vyh]], [[Resolution|resolution]] 3.40&Aring;' 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'>[[1vyh]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VYH 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">X-ray diffraction, [[Resolution|Resolution]] 3.4&#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=1vyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vyh OCA], [https://pdbe.org/1vyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vyh RCSB], [https://www.ebi.ac.uk/pdbsum/1vyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vyh ProSAT]</span></td></tr>
-
{{STRUCTURE_1vyh| PDB=1vyh | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PA1B2_HUMAN PA1B2_HUMAN] Inactivates PAF by removing the acetyl group at the sn-2 position. This is a catalytic subunit.
 +
== 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/vy/1vyh_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=1vyh ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Mutations in the LIS1 gene cause lissencephaly, a human neuronal migration disorder. LIS1 binds dynein and the dynein-associated proteins Nde1 (formerly known as NudE), Ndel1 (formerly known as NUDEL), and CLIP-170, as well as the catalytic alpha dimers of brain cytosolic platelet activating factor acetylhydrolase (PAF-AH). The mechanism coupling the two diverse regulatory pathways remains unknown. We report the structure of LIS1 in complex with the alpha2/alpha2 PAF-AH homodimer. One LIS1 homodimer binds symmetrically to one alpha2/alpha2 homodimer via the highly conserved top faces of the LIS1 beta propellers. The same surface of LIS1 contains sites of mutations causing lissencephaly and overlaps with a putative dynein binding surface. Ndel1 competes with the alpha2/alpha2 homodimer for LIS1, but the interaction is complex and requires both the N- and C-terminal domains of LIS1. Our data suggest that the LIS1 molecule undergoes major conformational rearrangement when switching from a complex with the acetylhydrolase to the one with Ndel1.
-
'''PAF-AH HOLOENZYME: LIS1/ALFA2'''
+
Coupling PAF signaling to dynein regulation: structure of LIS1 in complex with PAF-acetylhydrolase.,Tarricone C, Perrina F, Monzani S, Massimiliano L, Kim MH, Derewenda ZS, Knapp S, Tsai LH, Musacchio A Neuron. 2004 Dec 2;44(5):809-21. PMID:15572112<ref>PMID:15572112</ref>
-
 
+
-
 
+
-
==Overview==
+
-
Mutations in the LIS1 gene cause lissencephaly, a human neuronal migration disorder. LIS1 binds dynein and the dynein-associated proteins Nde1 (formerly known as NudE), Ndel1 (formerly known as NUDEL), and CLIP-170, as well as the catalytic alpha dimers of brain cytosolic platelet activating factor acetylhydrolase (PAF-AH). The mechanism coupling the two diverse regulatory pathways remains unknown. We report the structure of LIS1 in complex with the alpha2/alpha2 PAF-AH homodimer. One LIS1 homodimer binds symmetrically to one alpha2/alpha2 homodimer via the highly conserved top faces of the LIS1 beta propellers. The same surface of LIS1 contains sites of mutations causing lissencephaly and overlaps with a putative dynein binding surface. Ndel1 competes with the alpha2/alpha2 homodimer for LIS1, but the interaction is complex and requires both the N- and C-terminal domains of LIS1. Our data suggest that the LIS1 molecule undergoes major conformational rearrangement when switching from a complex with the acetylhydrolase to the one with Ndel1.
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
1VYH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VYH OCA].
+
</div>
 +
<div class="pdbe-citations 1vyh" style="background-color:#fffaf0;"></div>
-
==Reference==
+
==See Also==
-
Coupling PAF signaling to dynein regulation: structure of LIS1 in complex with PAF-acetylhydrolase., Tarricone C, Perrina F, Monzani S, Massimiliano L, Kim MH, Derewenda ZS, Knapp S, Tsai LH, Musacchio A, Neuron. 2004 Dec 2;44(5):809-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15572112 15572112]
+
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
-
[[Category: 1-alkyl-2-acetylglycerophosphocholine esterase]]
+
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Protein complex]]
+
[[Category: Derewenda ZS]]
-
[[Category: Derewenda, Z S.]]
+
[[Category: Knapp S]]
-
[[Category: Knapp, S.]]
+
[[Category: Massimiliano L]]
-
[[Category: Massimiliano, L.]]
+
[[Category: Monzani S]]
-
[[Category: Monzani, S.]]
+
[[Category: Musacchio A]]
-
[[Category: Musacchio, A.]]
+
[[Category: Perrina F]]
-
[[Category: Perrina, F.]]
+
[[Category: Tarricone C]]
-
[[Category: Tarricone, C.]]
+
[[Category: Tsai L-H]]
-
[[Category: Tsai, L H.]]
+
-
[[Category: Acetylhydrolase]]
+
-
[[Category: Cell division]]
+
-
[[Category: Cytoskeleton]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Lissencephaly]]
+
-
[[Category: Mitosis]]
+
-
[[Category: Neurogenesis]]
+
-
[[Category: Platelet activacting factor]]
+
-
[[Category: Regulator of cytoplasmic dynein]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:54:50 2008''
+

Current revision

PAF-AH Holoenzyme: Lis1/Alfa2

PDB ID 1vyh

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/1vyh"
Personal tools