1vyh: Difference between revisions
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|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] | |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> | ||
|GENE= | |GENE= | ||
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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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[[Category: regulator of cytoplasmic dynein]] | [[Category: regulator of cytoplasmic dynein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:28:40 2008'' | ||
Revision as of 00:28, 31 March 2008
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| , resolution 3.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | 1-alkyl-2-acetylglycerophosphocholine esterase, with EC number 3.1.1.47 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PAF-AH HOLOENZYME: LIS1/ALFA2
OverviewOverview
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 StructureAbout this Structure
1VYH is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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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- 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