1vyh

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[[Image:1vyh.gif|left|200px]]
[[Image:1vyh.gif|left|200px]]
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{{Structure
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|PDB= 1vyh |SIZE=350|CAPTION= <scene name='initialview01'>1vyh</scene>, resolution 3.4&Aring;
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The line below this paragraph, containing "STRUCTURE_1vyh", creates the "Structure Box" on the page.
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|SITE=
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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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{{STRUCTURE_1vyh| PDB=1vyh | SCENE= }}
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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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'''PAF-AH HOLOENZYME: LIS1/ALFA2'''
'''PAF-AH HOLOENZYME: LIS1/ALFA2'''
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[[Category: Tarricone, C.]]
[[Category: Tarricone, C.]]
[[Category: Tsai, L H.]]
[[Category: Tsai, L H.]]
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[[Category: acetylhydrolase]]
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[[Category: Acetylhydrolase]]
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[[Category: cell division]]
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[[Category: Cell division]]
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[[Category: cytoskeleton]]
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[[Category: Cytoskeleton]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: lissencephaly]]
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[[Category: Lissencephaly]]
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[[Category: mitosis]]
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[[Category: Mitosis]]
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[[Category: neurogenesis]]
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[[Category: Neurogenesis]]
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[[Category: platelet activacting factor]]
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[[Category: Platelet activacting factor]]
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[[Category: regulator of cytoplasmic dynein]]
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[[Category: Regulator of cytoplasmic dynein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:54:50 2008''
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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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Revision as of 09:54, 3 May 2008

Image:1vyh.gif

Template:STRUCTURE 1vyh

PAF-AH HOLOENZYME: LIS1/ALFA2


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

1VYH is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 12:54:50 2008

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OCA

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