1vyh
From Proteopedia
(Difference between revisions)
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- | [[ | + | ==PAF-AH HOLOENZYME: LIS1/ALFA2== |
+ | <StructureSection load='1vyh' size='340' side='right' caption='[[1vyh]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1vyh]] is a 20 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VYH FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fxw|1fxw]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1vyh RCSB], [http://www.ebi.ac.uk/pdbsum/1vyh PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == 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/chain_selection.php?pdb_ID=2ata 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. | ||
- | + | 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> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Platelet-activating factor acetylhydrolase|Platelet-activating factor acetylhydrolase]] | *[[Platelet-activating factor acetylhydrolase|Platelet-activating factor acetylhydrolase]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: 1-alkyl-2-acetylglycerophosphocholine esterase]] | [[Category: 1-alkyl-2-acetylglycerophosphocholine esterase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] |
Revision as of 21:41, 28 September 2014
PAF-AH HOLOENZYME: LIS1/ALFA2
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Categories: 1-alkyl-2-acetylglycerophosphocholine esterase | Homo sapiens | Mus musculus | Derewenda, Z S. | Knapp, S. | Massimiliano, L. | Monzani, S. | Musacchio, A. | Perrina, F. | Tarricone, C. | Tsai, L H. | Acetylhydrolase | Cell division | Cytoskeleton | Hydrolase | Lissencephaly | Mitosis | Neurogenesis | Platelet activacting factor | Regulator of cytoplasmic dynein