1vyh: Difference between revisions
New page: left|200px<br /> <applet load="1vyh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vyh, resolution 3.4Å" /> '''PAF-AH HOLOENZYME: L... |
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[[Image:1vyh.gif|left|200px]]<br /> | [[Image:1vyh.gif|left|200px]]<br /><applet load="1vyh" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1vyh, resolution 3.4Å" /> | caption="1vyh, resolution 3.4Å" /> | ||
'''PAF-AH HOLOENZYME: LIS1/ALFA2'''<br /> | '''PAF-AH HOLOENZYME: LIS1/ALFA2'''<br /> | ||
==Overview== | ==Overview== | ||
Mutations in the LIS1 gene cause lissencephaly, a human neuronal migration | 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== | ==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:// | 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]. | ||
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Derewenda, Z | [[Category: Derewenda, Z S.]] | ||
[[Category: Knapp, S.]] | [[Category: Knapp, S.]] | ||
[[Category: Massimiliano, L.]] | [[Category: Massimiliano, L.]] | ||
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[[Category: Perrina, F.]] | [[Category: Perrina, F.]] | ||
[[Category: Tarricone, C.]] | [[Category: Tarricone, C.]] | ||
[[Category: Tsai, L | [[Category: Tsai, L H.]] | ||
[[Category: acetylhydrolase]] | [[Category: acetylhydrolase]] | ||
[[Category: cell division]] | [[Category: cell division]] | ||
| Line 34: | Line 33: | ||
[[Category: regulator of cytoplasmic dynein]] | [[Category: regulator of cytoplasmic dynein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:38:37 2008'' | ||
Revision as of 13:38, 21 February 2008
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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. Active as 1-alkyl-2-acetylglycerophosphocholine esterase, with EC number 3.1.1.47 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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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 1-alkyl-2-acetylglycerophosphocholine esterase
- Homo sapiens
- Mus musculus
- Protein complex
- 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
