IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v389y1997i6650d10.1038_38947.html
   My bibliography  Save this article

Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin

Author

Listed:
  • Glen Spraggon
  • Stephen J. Everse
  • Russell F. Doolittle

    (Center for Molecular Genetics, University of California)

Abstract

In blood coagulation, units of the protein fibrinogen pack together to form a fibrin clot, but a crystal structure for fibrinogen is needed to understand how this is achieved. The structure of a core fragment (fragment D) from human fibrinogen has now been determined to 2.9 Å resolution. The 86K three-chained structure consists of a coiled-coil region and two homologous globular entities oriented at approximately 130 degrees to each other. Additionally, the covalently bound dimer of fragment D, known as ‘double-D’, was isolated from human fibrin, crystallized in the presence of a Gly-Pro-Arg-Pro-amide peptide ligand, which simulates the donor polymerization site, and its structure solved by molecular replacement with the model of fragment D.

Suggested Citation

  • Glen Spraggon & Stephen J. Everse & Russell F. Doolittle, 1997. "Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin," Nature, Nature, vol. 389(6650), pages 455-462, October.
    • Handle: RePEc:nat:nature:v:389:y:1997:i:6650:d:10.1038_38947
    DOI: 10.1038/38947
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/38947
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/38947?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Stephan Köhler & Friederike Schmid & Giovanni Settanni, 2015. "The Internal Dynamics of Fibrinogen and Its Implications for Coagulation and Adsorption," PLOS Computational Biology, Public Library of Science, vol. 11(9), pages 1-19, September.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:389:y:1997:i:6650:d:10.1038_38947. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.