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| [[Image:1cds.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1cds| PDB=1cds | SCENE= }} | | {{STRUCTURE_1cds| PDB=1cds | SCENE= }} |
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| '''STRUCTURE OF A SOLUBLE, GLYCOSYLATED FORM OF THE HUMAN COMPLEMENT REGULATORY PROTEIN CD59'''
| | ===STRUCTURE OF A SOLUBLE, GLYCOSYLATED FORM OF THE HUMAN COMPLEMENT REGULATORY PROTEIN CD59=== |
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| ==Overview==
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| BACKGROUND: CD59 is a cell-surface glycoprotein that protects host cells from complement-mediated lysis by binding to and preventing the normal functioning of the complement proteins C8 and/or C9 which form part of a membrane penetrating assembly called the membrane attack complex. CD59 has no structural similarity to other complement proteins, but is an example of a plasma protein domain type found also in murine Ly-6 proteins and the urokinase-type plasminogen activator receptor. RESULTS: CD59 was purified from human urine, retaining the N-glycan and at least some of the non-lipid component of the glycosylphosphatidylinositol membrane anchor. The three-dimensional structure of the protein component has been determined in the presence of the carbohydrate groups using two-dimensional NMR spectroscopy. The protein structure is well defined by the NMR data (root mean square deviation from the mean structure of 0.65 A for backbone atoms and no distance constraint violations greater than 0.4 A). Structure calculations were also carried out to model the orientation of the N-acetylglucosamine residue that is directly linked to Asn18. CONCLUSIONS: The main features of the protein structure are two antiparallel beta-sheets (a central one with three strands and another with two), a short helix that packs against the three-stranded beta-sheet, and a carboxy-terminal region that, although lacking regular secondary structure, is well defined and packs against the three-stranded beta-sheet, on the opposite face to the helix. We have used the structure, in combination with existing biochemical data, to identify residues that may be involved in C8 binding.
| | The line below this paragraph, {{ABSTRACT_PUBMED_7520819}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 7520819 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_7520819}} |
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| ==About this Structure== | | ==About this Structure== |
| 1CDS is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDS OCA]. | | 1CDS is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDS OCA]. |
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| ==Reference== | | ==Reference== |
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| [[Category: Neuhaus, D.]] | | [[Category: Neuhaus, D.]] |
| [[Category: Complement regulatory protein]] | | [[Category: Complement regulatory protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:37:06 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:36:14 2008'' |