Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
51
pubmed:dateCreated
1995-1-27
pubmed:abstractText
The amino-terminal fragment (ATF) of urokinase-type plasminogen activator (u-PA) is a two-domain protein which consists of a kringle and a growth factor domain (GFD). The dynamics of uniformly 15N-labeled ATF was examined by measuring the longitudinal (T1) and transverse (T2) 15N relaxation times and heteronuclear NOEs. The data were interpreted in terms of the model-independent spectral density function. The GFD was found to exhibit a high degree of anisotropy, whereas the kringle domain of ATF undergoes isotropic reorientation. This difference in anisotropy is best explained by the two domains moving independently such as differently shaped beads on a string. With the exception of the N- and C-terminal regions of the protein, the most flexible region of ATF was the seven-residue omega loop (N22-I28) of the GFD which has been implicated in the binding of u-PA to its receptor. The amides of the linker region between the domains displayed high values of the order parameter, indicating restricted motion on the picosecond time scale. This is in contrast to the flexible linker of calmodulin [Barbato et al. (1992) Biochemistry 31, 5269-5278], which displayed low values of S2 and unrestricted motion in the linker region.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15418-24
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Backbone dynamics of a two-domain protein: 15N relaxation studies of the amino-terminal fragment of urokinase-type plasminogen activator.
pubmed:affiliation
Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, Ilinois 60064.
pubmed:publicationType
Journal Article