Linked Life Data

20693682

Source:http://linkedlifedata.com/resource/pubmed/id/20693682

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 8
pubmed:dateCreated
2010-8-9
pubmed:abstractText
An antibody Fab fragment, AbD1556, was selected against the extracellular domain of BMP receptor type IA, which blocks the binding of BMP-2 to BMPR-IA and thereby neutralizes BMP-2 activity. To study the mechanism by which BMPR-IA is recognized and bound by the Fab fragment, the complex of AbD1556 bound to BMPR-IA was prepared and crystallized. Crystals of this binary complex belonged to the monoclinic space group P2(1), with unit-cell parameters a=89.32, b=129.25, c=100.24 A, beta=92.27 degrees.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1744-3091
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
66
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
964-8
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Crystallization of BMP receptor type IA bound to the antibody Fab fragment AbD1556.
pubmed:affiliation
Lehrstuhl für Physiologische Chemie II, Biozentrum der Universität Würzburg, Am Hubland, D-97074 Würzburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't