2mnu
From Proteopedia
Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for EDB and specific binding aptide
Structural highlights
DiseaseFINC_HUMAN Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:601894; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.[1] FunctionFINC_HUMAN Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.[2] [3] [4] [5] Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.[6] [7] [8] [9] Publication Abstract from PubMedAptides, a novel class of high-affinity peptides, recognize diverse molecular targets with high affinity and specificity. The solution structure of the aptide APT specifically bound to fibronectin extradomain B (EDB), which represents an unusual protein-protein interaction that involves coupled unfolding and binding, is reported. APT binding is accompanied by unfolding of the C-terminal beta strand of EDB, thereby permitting APT to interact with the freshly exposed hydrophobic interior surfaces of EDB. The beta-hairpin scaffold of APT drives the interaction by a beta-strand displacement mechanism, such that an intramolecular beta sheet is replaced by an intermolecular beta sheet. The unfolding of EDB perturbs the tight domain association between EDB and FN8 of fibronectin, thus highlighting its potential use as a scaffold that switches between stretched and bent conformations. An Unusual Protein-Protein Interaction through Coupled Unfolding and Binding.,Yu TK, Shin SA, Kim EH, Kim S, Ryu KS, Cheong H, Ahn HC, Jon S, Suh JY Angew Chem Int Ed Engl. 2014 Sep 8;53(37):9784-7. doi: 10.1002/anie.201404750., Epub 2014 Jul 1. PMID:24985319[10] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||
