Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 7
pubmed:dateCreated
2003-6-30
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1273-5
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Crystallization and initial crystal characterization of the N-terminal DH/PH domain of Trio.
pubmed:affiliation
Department of Physiology and Biophysics, Stony Brook University, Stony Brook, NY 11794-8661, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't