1ixa
From Proteopedia
(New page: 200px<br /> <applet load="1ixa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ixa" /> '''THE THREE-DIMENSIONAL STRUCTURE OF THE FIRS...) |
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| - | [[Image:1ixa.gif|left|200px]]<br /> | + | [[Image:1ixa.gif|left|200px]]<br /><applet load="1ixa" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ixa" size=" | + | |
caption="1ixa" /> | caption="1ixa" /> | ||
'''THE THREE-DIMENSIONAL STRUCTURE OF THE FIRST EGF-LIKE MODULE OF HUMAN FACTOR IX: COMPARISON WITH EGF AND TGF-A'''<br /> | '''THE THREE-DIMENSIONAL STRUCTURE OF THE FIRST EGF-LIKE MODULE OF HUMAN FACTOR IX: COMPARISON WITH EGF AND TGF-A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the first epidermal growth factor | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IXA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1IXA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IXA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Baron, M.]] | [[Category: Baron, M.]] | ||
| - | [[Category: Brownlee, G | + | [[Category: Brownlee, G G.]] |
| - | [[Category: Campbell, I | + | [[Category: Campbell, I D.C.]] |
| - | [[Category: Hanford, P | + | [[Category: Hanford, P A.]] |
| - | [[Category: Harvey, T | + | [[Category: Harvey, T S.]] |
[[Category: Mayhew, M.]] | [[Category: Mayhew, M.]] | ||
| - | [[Category: Norman, D | + | [[Category: Norman, D G.]] |
| - | [[Category: Tse, A | + | [[Category: Tse, A G.D.]] |
[[Category: human factor ix]] | [[Category: human factor ix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:16:39 2008'' |
Revision as of 11:16, 21 February 2008
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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
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