The structure of the Ca2+-binding, glycosylated F-spondin domain of F-spondin - A C2-domain variant in an extracellular matrix protein

BMC Structural Biology

Volumn 11, Issue , 2011, Pages

  Tan, Kemin ^a   Lawler, Jack ^b  

^a ARGONNE NATIONAL LABORATORY   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; DISULFIDE; F SPONDIN; INTEGRIN; SCLEROPROTEIN; SULFATE; UNCLASSIFIED DRUG; SPON1 PROTEIN, HUMAN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CALCIUM BINDING; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISULFIDE BOND; DROSOPHILA; NERVE FIBER; NONHUMAN; OPTICAL RESOLUTION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN GLYCOSYLATION; PROTEIN STRUCTURE; STRUCTURAL HOMOLOGY; CHEMISTRY; GLYCOSYLATION; HUMAN; MOLECULAR GENETICS; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BINDING SITES; CALCIUM; CRYSTALLOGRAPHY, X-RAY; DISULFIDES; EXTRACELLULAR MATRIX PROTEINS; GLYCOSYLATION; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 79955733040     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-11-22     Document Type: Article

References (39)

1. F-spondin: a gene expressed at high levels in the floor plate encodes a secreted protein that promotes neural cell adhesion and neurite extension. A Klar M Baldassare TM Jessell, Cell 1992 69 1 95 110 10.1016/0092-8674(92)90121-R 1555244
2. F-Spondin is required for accurate pathfinding of commissural axons at the floor plate. T Burstyn-Cohen V Tzarfaty A Frumkin Y Feinstein E Stoeckli A Klar, Neuron 1999 23 2 233 246 10.1016/S0896-6273(00)80776-X 10399931 (Pubitemid 29315720)
3. F-spondin and mindin: two structurally and functionally related genes expressed in the hippocampus that promote outgrowth of embryonic hippocampal neurons. Y Feinstein V Borrell C Garcia T Burstyn-Cohen V Tzarfaty A Frumkin A Nose H Okamoto S Higashijima E Soriano,, et al. Development (Cambridge, England) 1999 126 16 3637 3648 (Pubitemid 29419519)
4. F-Spondin, expressed in somite regions avoided by neural crest cells, mediates inhibition of distinct somite domains to neural crest migration. A Debby-Brafman T Burstyn-Cohen A Klar C Kalcheim, Neuron 1999 22 3 475 488 10.1016/S0896-6273(00)80703-5 10197528 (Pubitemid 29159847)
5. The crystal structure of the heparin-binding reelin-N domain of f-spondin. K Tan M Duquette JH Liu J Lawler JH Wang, Journal of molecular biology 2008 381 5 1213 1223 10.1016/j.jmb.2008.06.045 18602404
6. Proteolysis and membrane capture of F-spondin generates combinatorial guidance cues from a single molecule. S Zisman K Marom O Avraham L Rinsky-Halivni U Gai G Kligun V Tzarfaty-Majar T Suzuki A Klar, The Journal of cell biology 2007 178 7 1237 1249 10.1083/jcb.200702184 17875744 (Pubitemid 47480229)
7. F-spondin promotes nerve precursor differentiation. D Schubert A Klar M Park R Dargusch WH Fischer, Journal of neurochemistry 2006 96 2 444 453 10.1111/j.1471-4159.2005.03563.x 16300627
8. Isolation and characterization of vascular smooth muscle cell growth promoting factor from bovine ovarian follicular fluid and its cDNA cloning from bovine and human ovary. K Miyamoto Y Morishita M Yamazaki N Minamino K Kangawa H Matsuo T Mizutani K Yamada T Minegishi, Archives of biochemistry and biophysics 2001 390 1 93 100 10.1006/abbi.2001.2367 11368520 (Pubitemid 32493574)
9. The first large-scale nucleic acid amplification testing (NAT) of donated blood using multiplex reagent for simultaneous detection of HBV, HCV, and HIV-1 and significance of NAT for HBV. H Ohnuma T Tanaka A Yoshikawa H Murokawa K Minegishi R Yamanaka HY Lizuka M Miyamoto S Satoh S Nakahira,, et al. Microbiology and immunology 2001 45 9 667 672 11694079 (Pubitemid 32895926)
10. Vascular smooth muscle cell growth-promoting factor/F-spondin inhibits angiogenesis via the blockade of integrin alphavbeta3 on vascular endothelial cells. Y Terai M Abe K Miyamoto M Koike M Yamasaki M Ueda M Ueki Y Sato, Journal of cellular physiology 2001 188 3 394 402 10.1002/jcp.1122 11473366 (Pubitemid 32777181)
11. Effect of F-spondin on cementoblastic differentiation of human periodontal ligament cells. M Kitagawa Y Kudo S Iizuka I Ogawa Y Abiko M Miyauchi T Takata, Biochem Biophys Res Commun 2006 349 3 1050 1056 10.1016/j.bbrc.2006.08.142 16965763 (Pubitemid 44380203)
12. F-spondin, a neuroregulatory protein, is up-regulated in osteoarthritis and regulates cartilage metabolism via TGF-beta activation. MG Attur GD Palmer HE Al-Mussawir M Dave CC Teixeira DB Rifkin CT Appleton F Beier SB Abramson, Faseb J 2009 23 1 79 89 10.1096/fj.08-114363 18780763
13. Binding of F-spondin to amyloid-beta precursor protein: a candidate amyloid-beta precursor protein ligand that modulates amyloid-beta precursor protein cleavage. A Ho TC Sèudhof, Proceedings of the National Academy of Sciences of the United States of America 2004 101 8 2548 2553 10.1073/pnas.0308655100 14983046 (Pubitemid 38269348)
14. F-spondin interaction with the apolipoprotein E receptor ApoEr2 affects processing of amyloid precursor protein. HS Hoe D Wessner U Beffert AG Becker Y Matsuoka GW Rebeck, Molecular and cellular biology 2005 25 21 9259 9268 10.1128/MCB.25.21.9259-9268.2005 16227578 (Pubitemid 41507828)
15. Functional interactions of APP with the apoE receptor family. HS Hoe GW Rebeck, Journal of neurochemistry 2008 106 6 2263 2271 10.1111/j.1471-4159.2008. 05517.x 18554321
16. Structure of the F-spondin domain of mindin, an integrin ligand and pattern recognition molecule. Y Li C Cao W Jia L Yu M Mo Q Wang Y Huang JM Lim M Ishihara L Wells,, et al. The EMBO journal 2009 28 3 286 297 10.1038/emboj.2008.288 19153605
17. Mindin/F-spondin family: novel ECM proteins expressed in the zebrafish embryonic axis. S Higashijima A Nose G Eguchi Y Hotta H Okamoto, Developmental biology 1997 192 2 211 227 10.1006/dbio.1997.8760 9441663 (Pubitemid 28066929)
18. The extracellular matrix protein mindin is a pattern-recognition molecule for microbial pathogens. YW He H Li J Zhang CL Hsu E Lin N Zhang J Guo KA Forbush MJ Bevan, Nature immunology 2004 5 1 88 97 10.1038/ni1021 14691481 (Pubitemid 38081473)
19. Pattern recognition molecule mindin promotes intranasal clearance of influenza viruses. W Jia H Li YW He, Journal of immunology (Baltimore, Md:1950) 2008 180 9 6255 6261
20. Structure of the F-spondin reeler domain reveals a unique beta-sandwich fold with a deformable disulfide-bonded loop. M Nagae K Nishikawa N Yasui M Yamasaki T Nogi J Takagi, Acta crystallographica Section D, Biological crystallography 2008 64 Pt 1138 1145 19020352
21. Solution structures of the first and fourth TSR domains of F-spondin. K Pèaèakkèonen H Tossavainen P Permi H Rakkolainen H Rauvala E Raulo I Kilpelèainen P Gèuntert, Proteins 2006 64 3 665 672 10.1002/prot.21030 16736493 (Pubitemid 44100732)
22. C2-domains, structure and function of a universal Ca2+-binding domain. J Rizo TC Sèudhof, The Journal of biological chemistry 1998 273 26 15879 15882 10.1074/jbc.273.26.15879 9632630 (Pubitemid 28311347)
23. Phylogeny.fr: robust phylogenetic analysis for the non-specialist. A Dereeper V Guignon G Blanc S Audic S Buffet F Chevenet JF Dufayard S Guindon V Lefort M Lescot,, et al. Nucleic Acids Res 2008 36 Web Server 465 469
24. The crystal structure of the signature domain of cartilage oligomeric matrix protein: implications for collagen, glycosaminoglycan and integrin binding. K Tan M Duquette A Joachimiak J Lawler, Faseb J 2009 23 8 2490 2501 10.1096/fj.08-128090 19276170
25. The geometry of metal-ligand interactions relevant to proteins. MM Harding, Acta crystallographica Section D, Biological crystallography 1999 55 Pt 1432 1443 10417412 (Pubitemid 29395738)
26. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. E Krissinel K Henrick, Acta crystallographica Section D, Biological crystallography 2004 60 Pt 2256 2268 15572779 (Pubitemid 41742778)
27. Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism. A Dessen J Tang H Schmidt M Stahl JD Clark J Seehra WS Somers, Cell 1999 97 3 349 360 10.1016/S0092-8674(00)80744-8 10319815 (Pubitemid 29214591)
28. Membrane binding and subcellular targeting of C2 domains. W Cho RV Stahelin, Biochimica et biophysica acta 2006 1761 8 838 849 16945584 (Pubitemid 44332329)
29. DOC2B, C2 domains, and calcium: A tale of intricate interactions. R Friedrich A Yeheskel U Ashery, Mol Neurobiol 2010 41 1 42 51 10.1007/s12035-009-8094-8 20052564
30. Membrane association with multiple calcium ions: vitamin-K-dependent proteins, annexins and pentraxins. GL Nelsestuen BG Ostrowski, Curr Opin Struct Biol 1999 9 4 433 437 10.1016/S0959-440X(99)80060-8 10449363 (Pubitemid 29377884)
31. Thrombospondin-1 type 1 repeat recombinant proteins inhibit tumor growth through transforming growth factor-beta-dependent and -independent mechanisms. WM Miao WL Seng M Duquette P Lawler C Laus J Lawler, Cancer Res 2001 61 21 7830 7839 11691800 (Pubitemid 33049372)
32. HKL-3000: the integration of data reduction and structure solution - from diffraction images to an initial model in minutes. W Minor M Cymborowski Z Otwinowski M Chruszcz, Acta crystallographica Section D, Biological crystallography 2006 62 Pt 859 866 16855301 (Pubitemid 44125661)
33. MOLREP: an automated program for molecular replacement. AA Vagin A Teplyakov, J Appl Crystallogr 1997 30 1022 1025 10.1107/S0021889897006766 (Pubitemid 127485985)
34. Coot: model-building tools for molecular graphics. P Emsley K Cowtan, Acta crystallographica Section D, Biological crystallography 2004 60 Pt 2126 2132 15572765 (Pubitemid 41742764)
35. Refinement of macromolecular structures by the maximum-likelihood method. GN Murshudov AA Vagin EJ Dodson, Acta crystallographica Section D, Biological crystallography 1997 53 Pt 240 255 15299926 (Pubitemid 27235885)
36. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. IW Davis A Leaver-Fay VB Chen JN Block GJ Kapral X Wang LW Murray WB Arendall J Snoeyink JS Richardson,, et al. Nucleic Acids Res 2007 35 Web Server 375 383
37. MOLSCRIPT: A Program to Produce Both Detailed and Schematic Plots of Protein Structures. PJ Kraulis, J Appl Crystallogr 1991 24 946 950 10.1107/S0021889891004399
38. Multiple sequence alignment with hierarchical clustering. F Corpet, Nucleic Acids Res 1988 16 22 10881 10890 10.1093/nar/16.22.10881 2849754
39. ESPript: analysis of multiple sequence alignments in PostScript. P Gouet E Courcelle DI Stuart F Métoz, Bioinformatics 1999 15 4 305 308 10.1093/bioinformatics/15.4.305 10320398 (Pubitemid 29213756)