1cdr: Difference between revisions

Revision as of 20:36, 30 June 2008

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File:1cdr.png

Template:STRUCTURE 1cdr

STRUCTURE OF A SOLUBLE, GLYCOSYLATED FORM OF THE HUMAN COMPLEMENT REGULATORY PROTEIN CD59STRUCTURE OF A SOLUBLE, GLYCOSYLATED FORM OF THE HUMAN COMPLEMENT REGULATORY PROTEIN CD59

Template:ABSTRACT PUBMED 7520819

About this StructureAbout this Structure

1CDR is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

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

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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===
-==Overview==
+<!--
-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}}
 ==About this Structure==
-CDR is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDR OCA].
+CDR is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDR OCA].
 ==Reference==
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 [[Category: Neuhaus, D.]]
 [[Category: Complement regulatory protein]]
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