Prev. Article Next Article Table of Contents

Article

Crystal Structure of Fragment Double-D from Human Fibrin with Two Different Bound Ligands^†^,^‡

Addition/Correction

Stephen J. Everse,^§ Glen Spraggon,^§ Leela Veerapandian, Marcia Riley, and Russell F. Doolittle*

Center for Molecular Genetics, University of California, San Diego, La Jolla, California 92093-0634

Biochemistry, 1998, 37 (24), pp 8637–8642

DOI: 10.1021/bi9804129

Publication Date (Web): May 21, 1998

†

This work was supported by Grant HL-26873 from the National Heart, Lung & Blood Institute.

‡

Atomic coordinates are available from the Brookhaven Protein Data Bank under access code 1FZC.

These authors contributed equally to this work.

To whom correspondence should be addressed. Telephone: (619) 534-4417. Fax: (619) 534-4985. E-mail: rdoolittle@ucsd.edu.

Abstract

Factor XIII-cross-linked fragment D (double-D) from human fibrin was crystallized in the presence of two different peptide ligands and the X-ray structure determined at 2.3 Å. The peptide Gly-Pro-Arg-Pro-amide, which is an analogue of the knob exposed by the thrombin-catalyzed removal of fibrinopeptide A, was found to reside in the γ-chain holes, and the peptide Gly-His-Arg-Pro-amide, which corresponds to the β-chain knob, was found in the homologous β-chain holes. The structure shows for the first time that the β-chain knob does indeed bind to a homologous hole on the β-chain. The γ- and β-chain holes are structurally very similar, and it is remarkable they are able to distinguish between these two peptides that differ by a single amino acid. Additionally, we have found that the β-chain domain, like its γ-chain counterpart, binds calcium.

View: Full Text HTML | Hi-Res PDF