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Tytuł pozycji:

A 50-A separation of the integrin alpha v beta 3 extracellular domain C termini reveals an intermediate activation state.

Tytuł :
A 50-A separation of the integrin alpha v beta 3 extracellular domain C termini reveals an intermediate activation state.
Index Terms :
Sciences bio-médicales et agricoles
Biochimie
Biologie
Biologie cellulaire
Biologie moléculaire
Biophysique
Sciences biomédicales
Sciences de la matière vivante
Alkaline Phosphatase -- genetics
Alkaline Phosphatase -- metabolism
Binding Sites
Cell Membrane -- metabolism
Chromatography, Gel
Cytoplasm -- chemistry
Dimerization
Humans
Immunosorbent Techniques
Integrin alphaVbeta3 -- chemistry
Integrin alphaVbeta3 -- genetics
Integrin alphaVbeta3 -- physiology
Ligands
Models, Molecular
Molecular Structure
Molecular Weight
Peptide Fragments -- chemistry
Peptide Fragments -- genetics
Placenta -- enzymology
Protein Conformation
Recombinant Fusion Proteins -- chemistry
Recombinant Fusion Proteins -- metabolism
Transfection
info:eu-repo/semantics/article
info:ulb-repo/semantics/articlePeerReview
info:ulb-repo/semantics/openurl/article
Wydawca :
2004-12
Dodane szczegóły :
Gline, Stephanie E
Cambier, Stephanie
Govaerts, Cédric
Nishimura, Stephen L
Typ dokumentu :
Zasób elektroniczny
URL :
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/59091
http://worldcat.org/search?q=on:EQY+http://difusion-oai.ulb.ac.be/oai/request+DCG_ENTIRE_REPOSITORY+CNTCOLL
Dostępność :
Open access content. Open access content
2 full-text file(s): info:eu-repo/semantics/restrictedAccess | info:eu-repo/semantics/closedAccess
Pozostałe numery :
EQY oai:dipot.ulb.ac.be:2013/59091
uri/info:doi/10.1074/jbc.M406582200
uri/info:pii/M406582200
uri/info:pmid/15475365
https://dipot.ulb.ac.be/dspace/bitstream/2013/59091/4/doi_35294.pdf
https://dipot.ulb.ac.be/dspace/bitstream/2013/59091/1/Article 13.pdf
764599858
Źródło wspomagające :
UNIV LIBR DE BRUXELLES
From OAIster®, provided by the OCLC Cooperative.
Numer akcesji :
edsoai.ocn764599858
Zasób elektroniczny
The integrin alpha(v)beta(3) has been shown to exist in low and high affinity conformations. Activation to the high affinity state is thought to depend on the "switchblade-like" opening, from a low affinity bent conformation with a closed headpiece to an extended form of the integrin with an open headpiece. Activation has been shown to depend on separation of the cytoplasmic domains. How cytoplasmic domain separation is related to separation of the transmembrane domains is unknown, and the distance of separation of the transmembrane domains required for activation has not been defined. A constrained secreted form of alpha(v)beta(3) was engineered that introduced a 50-A separation of the integrin C-terminal tails of the extracellular domains of the alpha(v) and beta(3) subunits. Receptor binding and recognition by ligand-induced binding state (LIBS) monoclonal antibodies demonstrated that the mutant receptor was locked into a low affinity state that was likely in a partially extended conformation but with a closed headpiece. In the presence of RGD peptide, the constrained receptor was able to fully extend, as determined by full exposure of LIBS epitopes. In the presence of the appropriate LIBS antibody, high affinity ligand binding of the constrained receptor was achieved. The results support the existence of transient intermediate activation states of secreted alpha(v)beta(3). Furthermore, these results with the secreted alpha(v)beta(3) receptor support a model for the full-length membrane-bound form of alpha(v)beta(3), whereby a 50-A lateral separation of the integrin alpha(v) and beta(3) transmembrane domains would be sufficient to enforce the switchblade-like opening to the extended conformation but insufficient for full receptor activation.
Journal Article
Research Support, U.S. Gov't, P.H.S.
info:eu-repo/semantics/published

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