1vyh

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Revision as of 17:38, 12 November 2007

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spinqualitylabelsall models 1vyh, resolution 3.4Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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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