Linked Life Data

18466758

Source:http://linkedlifedata.com/resource/pubmed/id/18466758

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-12-29
pubmed:databankReference
pubmed:abstractText
Transport protein particle (TRAPP) is a large multiprotein complex that involves in ER-to-Golgi and intra-Golgi traffic. Synbindin, the human ortholog of yeast Trs23, is one component of the TRAPP complexes. In the hippocampal neurons the synbindin/syndecan complex is involved in synaptic membrane trafficking and thereby regulates the formation of dendritic spines. Here we present the three-dimensional structure of human synbindin, which contains a longin domain (LD) and an atypical PDZ domain (APD). In the crystal, synbindin forms a hexamer, in which the LD forms two different conformations and the APD is quite disordered. These conformational changes of synbindin suggest a possible interaction mode of the LD.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
16
pubmed:volume
378
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
338-43
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Crystal structure of human synbindin reveals two conformations of longin domain.
pubmed:affiliation
School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, PR China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't