From Proteopedia
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| - | [[Image:1cdr.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1cdr| PDB=1cdr | SCENE= }} | | {{STRUCTURE_1cdr| PDB=1cdr | 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== |
| - | 1CDR is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDR OCA]. | + | 1CDR is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDR 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 12:37:03 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:36:14 2008'' |
Revision as of 17:36, 30 June 2008
Template:STRUCTURE 1cdr
STRUCTURE OF A SOLUBLE, GLYCOSYLATED FORM OF THE HUMAN COMPLEMENT REGULATORY PROTEIN CD59
Template:ABSTRACT PUBMED 7520819
About this Structure
1CDR is a Single protein structure. Full experimental information is available from OCA.
Reference
Structure of a soluble, glycosylated form of the human complement regulatory protein CD59., Fletcher CM, Harrison RA, Lachmann PJ, Neuhaus D, Structure. 1994 Mar 15;2(3):185-99. PMID:7520819
Page seeded by OCA on Mon Jun 30 20:36:14 2008
