1ixa
From Proteopedia
|
THE THREE-DIMENSIONAL STRUCTURE OF THE FIRST EGF-LIKE MODULE OF HUMAN FACTOR IX: COMPARISON WITH EGF AND TGF-A
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Hemophilia B OMIM:[306900], Warfarin sensitivity OMIM:[306900]
About this Structure
1IXA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of the first EGF-like module of human factor IX: comparison with EGF and TGF-alpha., Baron M, Norman DG, Harvey TS, Handford PA, Mayhew M, Tse AG, Brownlee GG, Campbell ID, Protein Sci. 1992 Jan;1(1):81-90. PMID:1304885
Page seeded by OCA on Mon Nov 12 17:35:39 2007
