3qw9

Crystal structure of betaglycan ZP-C domainCrystal structure of betaglycan ZP-C domain

Structural highlights 3qw9 is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: , , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TGBR3_RAT Binds to TGF-beta. Could be involved in capturing and retaining TGF-beta for presentation to the signaling receptors. Publication Abstract from PubMed The zona pellucida (ZP) domain is a bipartite protein structural element comprised of ZP-N and ZP-C regions. Most notable for its ability to mediate protein polymerization, many ZP proteins polymerize and assemble into long fibrils that form specialized extracellular matrices. Other ZP proteins (namely, betaglycan and endoglin) do not polymerize but serve as important membrane coreceptors for ligands in the transforming growth factor-beta (TGF-beta) superfamily. Here, we present the 2.0-A resolution crystal structure of the betaglycan ZP-C region in combination with a downstream region known as the external hydrophobic patch (EHP). Similar to the ZP-N region, the ZP-C region also adopts an immunoglobulin-like fold, despite sharing no sequence homology and possessing different disulfide linkages. The EHP region, which was previously thought to be external to the ZP region, is integral to the ZP-C domain and corresponds to the ZP-C G strand. Our structure also indicates that the critical maturation cleavage of ZP proteins, a process that activates nascent ZP proteins for polymerization, occurs within the immunoglobulin domain at the FG loop. Nonpolymerizing ZP proteins such as betaglycan and endoglin do not contain this cleavage site. Finally, our structure suggests that the AB loop and the convex surface pocket are regions important for TGF-beta ligand binding. Structure of betaglycan zona pellucida (ZP)-C domain provides insights into ZP-mediated protein polymerization and TGF-{beta} binding.,Lin SJ, Hu Y, Zhu J, Woodruff TK, Jardetzky TS Proc Natl Acad Sci U S A. 2011 Mar 29;108(13):5232-6. Epub 2011 Mar 14. PMID:21402931 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also TGF-beta receptor 3D structures

spinqualitylabelsall models 3qw9, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image