1xku

Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan

spinqualitylabelsall models 1xku, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1xku is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.15Å Ligands: NAG, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PGS2_BOVIN May affect the rate of fibrils formation. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Decorin is a ubiquitous extracellular matrix proteoglycan with a variety of important biological functions that are mediated by its interactions with extracellular matrix proteins, cytokines, and cell surface receptors. Decorin is the prototype of the family of small leucine-rich repeat proteoglycans and proteins (SLRPs), characterized by a protein core composed of leucine-rich repeats (LRRs), flanked by two cysteine-rich regions. We report here the crystal structure of the dimeric protein core of decorin, the best characterized member of the SLRP family. Each monomer adopts the curved solenoid fold characteristic of LRR domains, with a parallel beta-sheet on the inside interwoven with loops containing short segments of beta-strands, 3(10) helices, and polyproline II helices on the outside. Two main features are unique to this structure. First, decorin dimerizes through the concave surfaces of the LRR domains, which have been implicated previously in protein-ligand interactions. The amount of surface buried in this dimer rivals the buried surfaces of some of the highest-affinity macromolecular complexes reported to date. Second, the C-terminal region adopts an unusual capping motif that involves a laterally extended LRR and a disulfide bond. This motif seems to be unique to SLRPs and has not been observed in any other LRR protein structure to date. Possible implications of these features for decorin ligand binding and SLRP function are discussed. Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan.,Scott PG, McEwan PA, Dodd CM, Bergmann EM, Bishop PN, Bella J Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15633-8. Epub 2004 Oct 22. PMID:15501918 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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