6mzp

Zebrafish betaglycan orphan domain structure from orthorhombic crystal form

spinqualitylabelsall models 6mzp, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6mzp is a 2 chain structure with sequence from Danio rerio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E7FDB6_DANRE Publication Abstract from PubMed Betaglycan (BG) and endoglin (ENG), homologous co-receptors of the TGF-beta family, potentiate the signaling activity of TGF-beta2 and inhibin A, and BMP-9 and BMP-10, respectively. BG exists as monomer and forms 1:1 growth factor (GF) complexes, while ENG exists as a dimer and forms 2:1 GF complexes. Herein, the structure of the BG orphan domain (BGO) reveals an insertion that blocks the region that the endoglin orphan domain (ENGO) uses to bind BMP-9, preventing it from binding in the same manner. Using binding studies with domain-deleted forms of TGF-beta and BGO, as well as small-angle X-ray scattering data, BGO is shown to bind its cognate GF in an entirely different manner compared with ENGO. The alternative interfaces likely engender BG and ENG with the ability to selectively bind and target their cognate GFs in a unique temporal-spatial manner, without interfering with one another or other TGF-beta family GFs. Structural Adaptation in Its Orphan Domain Engenders Betaglycan with an Alternate Mode of Growth Factor Binding Relative to Endoglin.,Kim SK, Whitley MJ, Krzysiak TC, Hinck CS, Taylor AB, Zwieb C, Byeon CH, Zhou X, Mendoza V, Lopez-Casillas F, Furey W, Hinck AP Structure. 2019 Jul 16. pii: S0969-2126(19)30231-X. doi:, 10.1016/j.str.2019.06.010. PMID:31327662 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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