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1vyh

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[[Image:1vyh.gif|left|200px]]
 
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{{Structure
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==PAF-AH Holoenzyme: Lis1/Alfa2==
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|PDB= 1vyh |SIZE=350|CAPTION= <scene name='initialview01'>1vyh</scene>, resolution 3.4&Aring;
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<StructureSection load='1vyh' size='340' side='right'caption='[[1vyh]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/1-alkyl-2-acetylglycerophosphocholine_esterase 1-alkyl-2-acetylglycerophosphocholine esterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.47 3.1.1.47] </span>
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</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>
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|GENE=
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<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>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vyh OCA], [http://www.ebi.ac.uk/pdbsum/1vyh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vyh RCSB]</span>
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[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.
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vy/1vyh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1vyh ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''PAF-AH HOLOENZYME: LIS1/ALFA2'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1vyh" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==Reference==
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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]
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[[Category: 1-alkyl-2-acetylglycerophosphocholine esterase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Protein complex]]
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[[Category: Derewenda ZS]]
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[[Category: Derewenda, Z S.]]
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[[Category: Knapp S]]
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[[Category: Knapp, S.]]
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[[Category: Massimiliano L]]
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[[Category: Massimiliano, L.]]
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[[Category: Monzani S]]
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[[Category: Monzani, S.]]
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[[Category: Musacchio A]]
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[[Category: Musacchio, A.]]
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[[Category: Perrina F]]
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[[Category: Perrina, F.]]
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[[Category: Tarricone C]]
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[[Category: Tarricone, C.]]
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[[Category: Tsai L-H]]
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[[Category: Tsai, L H.]]
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[[Category: acetylhydrolase]]
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[[Category: cell division]]
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[[Category: cytoskeleton]]
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[[Category: hydrolase]]
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[[Category: lissencephaly]]
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[[Category: mitosis]]
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[[Category: neurogenesis]]
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[[Category: platelet activacting factor]]
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[[Category: regulator of cytoplasmic dynein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:28:40 2008''
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Current revision

PAF-AH Holoenzyme: Lis1/Alfa2

PDB ID 1vyh

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