InterPro

Literature: PAN/Apple domain (IPR003609)

References used in this entry

• Domains of invasion organelle proteins from apicomplexan parasites are homologous with the Apple domains of blood coagulation factor XI and plasma pre-kallikrein and are members of the PAN module superfamily.
  Brown PJ, Gill AC, Nugent PG, McVey JH, Tomley FM.
  FEBS Lett. 497 31-8 2001
  PMID: 11376658 Related citations
• The PAN module: the N-terminal domains of plasminogen and hepatocyte growth factor are homologous with the apple domains of the prekallikrein family and with a novel domain found in numerous nematode proteins.
  Tordai H, Banyai L, Patthy L.
  FEBS Lett. 461 63-7 1999
  PMID: 10561497 Related citations
• A binding site for heparin in the apple 3 domain of factor XI.
  Ho DH, Badellino K, Baglia FA, Walsh PN.
  J. Biol. Chem. 273 16382-90 1998
  PMID: 9632702 Related citations
• The solution structure of the N-terminal domain of hepatocyte growth factor reveals a potential heparin-binding site.
  Zhou H, Mazzulla MJ, Kaufman JD, Stahl SJ, Wingfield PT, Rubin JS, Bottaro DP, Byrd RA.
  Structure 6 109-16 1998
  PMID: 9493272 Related citations
• Mapping of the discontinuous kininogen binding site of prekallikrein. A distal binding segment is located in the heavy chain domain A4.
  Herwald H, Renne T, Meijers JC, Chung DW, Page JD, Colman RW, Muller-Esterl W.
  J. Biol. Chem. 271 13061-7 1996
  PMID: 8662705 Related citations
• Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule.
  McMullen BA, Fujikawa K, Davie EW.
  Biochemistry 30 2050-6 1991
  PMID: 1998666 Related citations
• Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.
  McMullen BA, Fujikawa K, Davie EW.
  Biochemistry 30 2056-60 1991
  PMID: 1998667 Related citations

Further reading

• Crystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor.
  Lietha D, Chirgadze DY, Mulloy B, Blundell TL, Gherardi E.
  EMBO J. 20 5543-55 2001
  PMID: 11597998 Related citations
• Crystal structure of the NK1 fragment of HGF/SF suggests a novel mode for growth factor dimerization and receptor binding.
  Chirgadze DY, Hepple JP, Zhou H, Byrd RA, Blundell TL, Gherardi E.
  Nat. Struct. Biol. 6 72-9 1999
  PMID: 9886295 Related citations
• A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist.
  Tolbert WD, Daugherty J, Gao C, Xie Q, Miranti C, Gherardi E, Woude GV, Xu HE.
  Proc. Natl. Acad. Sci. U.S.A. 104 14592-7 2007
  PMID: 17804794 Related citations
• A new crystal form of the NK1 splice variant of HGF/SF demonstrates extensive hinge movement and suggests that the NK1 dimer originates by domain swapping.
  Watanabe K, Chirgadze DY, Lietha D, de Jonge H, Blundell TL, Gherardi E.
  J. Mol. Biol. 319 283-8 2002
  PMID: 12051906 Related citations
• Solution structure of a PAN module from the apicomplexan parasite Eimeria tenella.
  Brown PJ, Mulvey D, Potts JR, Tomley FM, Campbell ID.
  J. Struct. Funct. Genomics 4 227-34 2003
  PMID: 15185963 Related citations