1fzd
From Proteopedia
(New page: 200px<br /> <applet load="1fzd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fzd, resolution 2.1Å" /> '''STRUCTURE OF RECOMBI...) |
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| - | [[Image:1fzd.gif|left|200px]]<br /> | + | [[Image:1fzd.gif|left|200px]]<br /><applet load="1fzd" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1fzd" size=" | + | |
caption="1fzd, resolution 2.1Å" /> | caption="1fzd, resolution 2.1Å" /> | ||
'''STRUCTURE OF RECOMBINANT ALPHAEC DOMAIN FROM HUMAN FIBRINOGEN-420'''<br /> | '''STRUCTURE OF RECOMBINANT ALPHAEC DOMAIN FROM HUMAN FIBRINOGEN-420'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a recombinant alphaEC domain from human | + | The crystal structure of a recombinant alphaEC domain from human fibrinogen-420 has been determined at a resolution of 2.1 A. The protein, which corresponds to the carboxyl domain of the alphaE chain, was expressed in and purified from Pichia pastoris cells. Felicitously, during crystallization an amino-terminal segment was removed, apparently by a contaminating protease, allowing the 201-residue remaining parent body to crystallize. An x-ray structure was determined by molecular replacement. The electron density was clearly defined, partly as a result of averaging made possible by there being eight molecules in the asymmetric unit related by noncrystallographic symmetry (P1 space group). Virtually all of an asparagine-linked sugar cluster is present. Comparison with structures of the beta- and gamma-chain carboxyl domains of human fibrinogen revealed that the binding cleft is essentially neutral and should not bind Gly-Pro-Arg or Gly-His-Arg peptides of the sort bound by those other domains. Nonetheless, the cleft is clearly evident, and the possibility of binding a carbohydrate ligand like sialic acid has been considered. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FZD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1FZD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FZD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Applegate, D.]] | [[Category: Applegate, D.]] | ||
| - | [[Category: Doolittle, R | + | [[Category: Doolittle, R F.]] |
| - | [[Category: Everse, S | + | [[Category: Everse, S J.]] |
[[Category: Grieninger, G.]] | [[Category: Grieninger, G.]] | ||
[[Category: Redman, C.]] | [[Category: Redman, C.]] | ||
[[Category: Spraggon, G.]] | [[Category: Spraggon, G.]] | ||
[[Category: Veerapandian, L.]] | [[Category: Veerapandian, L.]] | ||
| - | [[Category: Zhang, J | + | [[Category: Zhang, J Z.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: NAG]] | [[Category: NAG]] | ||
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[[Category: glycosylated protein]] | [[Category: glycosylated protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:44:19 2008'' |
Revision as of 10:44, 21 February 2008
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STRUCTURE OF RECOMBINANT ALPHAEC DOMAIN FROM HUMAN FIBRINOGEN-420
Contents |
Overview
The crystal structure of a recombinant alphaEC domain from human fibrinogen-420 has been determined at a resolution of 2.1 A. The protein, which corresponds to the carboxyl domain of the alphaE chain, was expressed in and purified from Pichia pastoris cells. Felicitously, during crystallization an amino-terminal segment was removed, apparently by a contaminating protease, allowing the 201-residue remaining parent body to crystallize. An x-ray structure was determined by molecular replacement. The electron density was clearly defined, partly as a result of averaging made possible by there being eight molecules in the asymmetric unit related by noncrystallographic symmetry (P1 space group). Virtually all of an asparagine-linked sugar cluster is present. Comparison with structures of the beta- and gamma-chain carboxyl domains of human fibrinogen revealed that the binding cleft is essentially neutral and should not bind Gly-Pro-Arg or Gly-His-Arg peptides of the sort bound by those other domains. Nonetheless, the cleft is clearly evident, and the possibility of binding a carbohydrate ligand like sialic acid has been considered.
Disease
Known diseases associated with this structure: Afibrinogenemia, congenital OMIM:[134820], Amyloidosis, hereditary renal OMIM:[134820], Dysfibrinogenemia, alpha type, causing bleeding diathesis OMIM:[134820], Dysfibrinogenemia, alpha type, causing recurrent thrombosis OMIM:[134820]
About this Structure
1FZD is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a recombinant alphaEC domain from human fibrinogen-420., Spraggon G, Applegate D, Everse SJ, Zhang JZ, Veerapandian L, Redman C, Doolittle RF, Grieninger G, Proc Natl Acad Sci U S A. 1998 Aug 4;95(16):9099-104. PMID:9689040
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