Thrombin Functions through Its RGD Sequence in a Non-canonical Conformation
نویسندگان
چکیده
منابع مشابه
Guessing and non-guessing of canonical functions
It is possible to control to a large extent, via semiproper forcing, the parameters (β0, β1) measuring the guessing density of the members of any given antichain of stationary subsets of ω1 (assuming the existence of an inaccessible limit of measurable cardinals). Here, given a pair (β0, β1) of ordinals, we will say that a stationary set S ⊆ ω1 has guessing density (β0, β1) if β0 = γ(S) and β1 ...
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The activating effect of Na(+) on thrombin is allosteric and depends on the conformational transition from a low activity Na(+)-free (slow) form to a high activity Na(+)-bound (fast) form. The structures of these active forms have been solved. Recent structures of thrombin obtained in the absence of Na(+) have also documented inactive conformations that presumably exist in equilibrium with the ...
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The P2Y 2 nucleotide receptor (P2Y 2 R) contains the integrin-binding domain arginine-glycineaspartic acid (RGD) in its first extracellular loop, raising the possibility that this G protein–coupled receptor interacts directly with an integrin. Binding of a peptide corresponding to the first extracellular loop of the P2Y 2 R to K562 erythroleukemia cells was inhibited by antibodies against a V b...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2005
ISSN: 0021-9258
DOI: 10.1074/jbc.c500248200