1vyh: Difference between revisions

Revision as of 04:01, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1vyh.png

Template:STRUCTURE 1vyh

PAF-AH HOLOENZYME: LIS1/ALFA2PAF-AH HOLOENZYME: LIS1/ALFA2

Template:ABSTRACT PUBMED 15572112

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

Page seeded by OCA on Mon Jul 28 04:01:37 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1vyh.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1vyh|  PDB=1vyh  |  SCENE=  }}
-'''PAF-AH HOLOENZYME: LIS1/ALFA2'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15572112}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15572112 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15572112}}
 ==About this Structure==
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 [[Category: Platelet activacting factor]]
 [[Category: Regulator of cytoplasmic dynein]]
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