Literature DB >> 12832783

Crystallization and initial crystal characterization of the N-terminal DH/PH domain of Trio.

Karlheinz Skowronek1, Mohammed Ghumman, Yi Zheng, Nicolas Nassar.   

Abstract

Trio is a multidomain signaling protein that plays an important role in neurite outgrowth, axon guidance and skeletal muscle development. Trio contains two DH/PH tandem domains that respectively activate the small GTPases RhoG/Rac and RhoA. The N-terminal DH/PH domain, TrioN, crystallizes in space group P3(1)21, with one TrioN molecule in the asymmetric unit and diffracts to 1.7 A resolution. The unit-cell parameters are a = b = 99.5, c = 98.3 A, alpha = beta = 90, gamma = 120 degrees. A greater than 90% complete native data set has been collected and structure determination using the multiple isomorphous replacement (MIR) method is ongoing.

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Year:  2003        PMID: 12832783     DOI: 10.1107/s0907444903009442

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  The DH and PH domains of Trio coordinately engage Rho GTPases for their efficient activation.

Authors:  Mariya K Chhatriwala; Laurie Betts; David K Worthylake; John Sondek
Journal:  J Mol Biol       Date:  2007-02-22       Impact factor: 5.469

  1 in total

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