1IXA

THE THREE-DIMENSIONAL STRUCTURE OF THE FIRST EGF-LIKE MODULE OF HUMAN FACTOR IX: COMPARISON WITH EGF AND TGF-A

Summary for 1IXA

• Entry DOI: 10.2210/pdb1ixa/pdb
• Descriptor: EGF-LIKE MODULE OF HUMAN FACTOR IX (1 entity in total)
• Functional Keywords: human factor ix
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P00740
• Total number of polymer chains: 1
• Total formula weight: 4279.64

Authors

Baron, M.,Norman, D.G.,Harvey, T.S.,Hanford, P.A.,Mayhew, M.,Tse, A.G.D.,Brownlee, G.G.,Campbell, I.D.C. (deposition date: 1991-11-14, release date: 1993-10-31, Last modification date: 2024-10-30)

Primary citation

Baron, M.,Norman, D.G.,Harvey, T.S.,Handford, P.A.,Mayhew, M.,Tse, A.G.,Brownlee, G.G.,Campbell, I.D.
The three-dimensional structure of the first EGF-like module of human factor IX: comparison with EGF and TGF-alpha.
Protein Sci., 1:81-90, 1992

PubMed Abstract: The three-dimensional structure of the first epidermal growth factor (EGF)-like module from human factor IX has been determined in solution using two-dimensional nuclear magnetic resonance (in the absence of calcium and at pH 4.5). The structure was found to resemble closely that of EGF and the homologous transforming growth factor-alpha (TGF-alpha). Residues 60-65 form an antiparallel beta-sheet with residues 68-73. In the C-terminal subdomain a type II beta-turn is found between residues 74 and 77 and a five-residue turn is found between residues 79 and 83. Glu 78 and Leu 84 pair in an antiparallel beta-sheet conformation. In the N-terminal region a loop is found between residues 50 and 55 such that the side chains of both are positioned above the face of the beta-sheet. Residues 56-60 form a turn that leads into the first strand of the beta-sheet. Whereas the global fold closely resembles that of EGF, the N-terminal residues of the module (46-49) do not form a beta-strand but are ill-defined in the structure, probably due to the local flexibility of this region. The structure is discussed with reference to recent site-directed mutagenesis data, which have identified certain conserved residues as ligands for calcium.

PubMed: 1304885

Experimental method

SOLUTION NMR