1ixa: Difference between revisions

Revision as of 14:09, 1 July 2008

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File:1ixa.png

Template:STRUCTURE 1ixa

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

Template:ABSTRACT PUBMED 1304885

About this StructureAbout this Structure

1IXA is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

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 Tue Jul 1 14:09:54 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1ixa.gif|left|200px]]
+{{Seed}}
+[[Image:1ixa.png|left|200px]]
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 {{STRUCTURE_1ixa|  PDB=1ixa  |  SCENE=  }}
-'''THE THREE-DIMENSIONAL STRUCTURE OF THE FIRST EGF-LIKE MODULE OF HUMAN FACTOR IX: COMPARISON WITH EGF AND TGF-A'''
+===THE THREE-DIMENSIONAL STRUCTURE OF THE FIRST EGF-LIKE MODULE OF HUMAN FACTOR IX: COMPARISON WITH EGF AND TGF-A===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_1304885}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 1304885 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_1304885}}
 ==About this Structure==
-IXA is a [[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].
+IXA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IXA OCA].
 ==Reference==
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 [[Category: Tse, A G.D.]]
 [[Category: Human factor ix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:32:16 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 14:09:54 2008''