@article{f1f84a4ff03746ed898452b9bc395179,
title = "Crystal structure of tandem type III fiibronectin domains from drosophila neuroglian at 2.0 {\aa}",
abstract = "We report the crystal structure of two adjacent fibronectin type III repeats from the Drosophila neural cell adhesion molecule neuroglian. Each domain consists of two antiparallel 0 sheets and is folded topologically identically to single fibronectin type III domains from the extracellular matrix proteins tenascin and fibronectin. β bulges and left-handed polyproline II helices disrupt the regular β sheet structure of both neuroglian domains. The hydrophobic interdomain interface includes a metalbinding site, presumably involved in stabilizing the relative orientation between domains and predicted by sequence comparision to be present in the vertebrate homolog molecule L1. The neuroglian domains are related by a near perfect 2-fold screw axis along the longest molecular dimension. Using this relationship, a model for arrays of tandem fibronectin type III repeats in neuroglian and other molecules is proposed.",
author = "Huber, {Andrew H.} and Wang, {Yu mei Eureka} and Bieber, {Allan J.} and Bjorkman, {Pamela J.}",
note = "Funding Information: We thank Michael Blum for help with freezing crystals; Michael Blum and the staff at CHESS for assistance with data collection; Alfonso Mondragdn for programs and advice during data processing; Barbara Hsu for her Patterson search program; Art Chir-ino and Bill Weis for advice during refinement; Dan Leahy, Wayne Hendrickson, and Harold Erickson for the TnFn3 coordinates and many helpful discussions; Abraham De Vos for the human growth hormone receptor coordinates; Bill Lane and the Harvard Microchemical Facility for mass spec and other analyses; the Caltech Microchemical Facility for N-terminal sequenceanal-yses; Peer Bork for aligned sequences of Fn-Ill repeats; Roland Strong for making Figure 38; Douglas Rees for helpful discussions about metal sites; and our colleagues for critical reading of the manuscript. The program X-PLORwas run on a CRAY-YMP at the San Diego Supercomputer Center, supported by the National Science Foundation. This work was supported by the Howard Hughes Medical Institute (P. J. B.), a Howard Hughes Medical Institute predoctoral fellowship (A. H. H.), the National Science Foundation (IBN-9128981 to A. J. B.), the American Cancer Society (IRG IN-17 to A. J. B.), and the Purdue Research Foundation (A. J. B.).",
year = "1994",
month = apr,
doi = "10.1016/0896-6273(94)90326-3",
language = "English (US)",
volume = "12",
pages = "717--731",
journal = "Neuron",
issn = "0896-6273",
publisher = "Cell Press",
number = "4",
}