1EDM

EPIDERMAL GROWTH FACTOR-LIKE DOMAIN FROM HUMAN FACTOR IX

Summary for 1EDM

• Entry DOI: 10.2210/pdb1edm/pdb
• Descriptor: FACTOR IX, CALCIUM ION (3 entities in total)
• Functional Keywords: epidermal growth factor, egf, calcium-binding, egf-like domain, structure and function, human factor ix, coagulation factor
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P00740
• Total number of polymer chains: 2
• Total formula weight: 8679.50

Authors

Rao, Z.,Handford, P.,Mayhew, M.,Knott, V.,Brownlee, G.G.,Stuart, D. (deposition date: 1996-03-21, release date: 1996-10-14, Last modification date: 2024-10-09)

Primary citation

Rao, Z.,Handford, P.,Mayhew, M.,Knott, V.,Brownlee, G.G.,Stuart, D.
The structure of a Ca(2+)-binding epidermal growth factor-like domain: its role in protein-protein interactions.
Cell(Cambridge,Mass.), 82:131-141, 1995

PubMed Abstract: Various diverse extracellular proteins possess Ca(2+)-binding epidermal growth factor (EGF)-like domains, the function of which remains uncertain. We have determined, at high resolution (1.5 A), the crystal structure of such a domain, from human clotting factor IX, as a complex with Ca2+. The Ca2+ ligands form a classic pentagonal bipyramid with six ligands contributed by one polypeptide chain and the seventh supplied by a neighboring EGF-like domain. The crystal structure identifies the role of Ca2+ in maintaining the conformation of the N-terminal region of the domain, but more importantly demonstrates that Ca2+ can directly mediate protein-protein contacts. The observed crystal packing of the domains provides a plausible model for the association of multiple tandemly linked EGF-like domains in proteins such as fibrillin-1, Notch, and protein S. This model is consistent with the known functional data and suggests a general biological role for these domains.

PubMed: 7606779
DOI: 10.1016/0092-8674(95)90059-4

Experimental method

X-RAY DIFFRACTION (1.5 Å)