Pub. Date : 1991 Mar 1
PMID : 1706595
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Endogenous cleavage of the Arg-379-Ala-380 bond in vitronectin results in a distinct conformational change which "buries" Ser-378, its site of phosphorylation by protein kinase A. Activation of blood platelets by thrombin was previously shown to specifically release protein kinase A, which in human plasma singles out and phosphorylates one protein, identified as vitronectin. | Serine | vitronectin | Homo sapiens |
| 2 | Endogenous cleavage of the Arg-379-Ala-380 bond in vitronectin results in a distinct conformational change which "buries" Ser-378, its site of phosphorylation by protein kinase A. Activation of blood platelets by thrombin was previously shown to specifically release protein kinase A, which in human plasma singles out and phosphorylates one protein, identified as vitronectin. | Serine | vitronectin | Homo sapiens |
| 3 | 1 mol/mol), that it is targeted to one site (Ser-378) at the C-terminal edge of the heparin-binding domain, and that it distinguishes between the two physiologically occurring forms of vitronectin: the one-chain (75 kDa) form, and the nicked two-chain (65 + 10 kDa) form, held together by an interchain disulphide bridge. | Serine | vitronectin | Homo sapiens |
| 4 | Cleavage of the Arg-379-Ala-380 bond results therefore in a conformationally distinct form of vitronectin in which Ser-378 is "buried". | Serine | vitronectin | Homo sapiens |
| 5 | This is demonstrated by our finding that Ser-378 is present in the 65 kDa chain of clipped vitronectin but inaccessible to phosphorylation at physiological pH. | Serine | vitronectin | Homo sapiens |