1vyh: Difference between revisions

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[[Image:1vyh.gif|left|200px]]<br /><applet load="1vyh" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1vyh.gif|left|200px]]
caption="1vyh, resolution 3.4&Aring;" />
 
'''PAF-AH HOLOENZYME: LIS1/ALFA2'''<br />
{{Structure
|PDB= 1vyh |SIZE=350|CAPTION= <scene name='initialview01'>1vyh</scene>, resolution 3.4&Aring;
|SITE=
|LIGAND=
|ACTIVITY= [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]
|GENE=
}}
 
'''PAF-AH HOLOENZYME: LIS1/ALFA2'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1VYH is a [http://en.wikipedia.org/wiki/Protein_complex 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]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VYH OCA].  
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].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15572112 15572112]
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]
[[Category: 1-alkyl-2-acetylglycerophosphocholine esterase]]
[[Category: 1-alkyl-2-acetylglycerophosphocholine esterase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: regulator of cytoplasmic dynein]]
[[Category: regulator of cytoplasmic dynein]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:38:37 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:49:44 2008''

Revision as of 12:49, 20 March 2008

File:1vyh.gif


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1vyh, resolution 3.4Å
Activity: 1-alkyl-2-acetylglycerophosphocholine esterase, with EC number 3.1.1.47
Coordinates: save as pdb, mmCIF, xml



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

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