PDBsum entry 1cdr

Complement regulatory protein

PDB id: 1cdr

Contents

Protein chain

77 a.a. *

Ligands

NAG-NAG-FUC

* Residue conservation analysis

PDB id:

1cdr

Name:

Complement regulatory protein

Title:

Structure of a soluble, glycosylated form of the human complement regulatory protein cd59

Structure:

Cd59. Chain: a. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606

NMR struc:

10 models

Authors:

C.M.Fletcher,R.A.Harrison,P.J.Lachmann,D.Neuhaus

Key ref:

C.M.Fletcher et al. (1994). Structure of a soluble, glycosylated form of the human complement regulatory protein CD59. Structure, 2, 185-199. PubMed id: 7520819 DOI: 10.1016/S0969-2126(00)00020-4

Date:

01-Jun-94 Release date: 30-Sep-94

Protein chain

P13987  (CD59_HUMAN) -  CD59 glycoprotein from Homo sapiens

Seq: 128 a.a.

Struc: 77 a.a.

DOI no: 10.1016/S0969-2126(00)00020-4

Structure 2:185-199 (1994)

PubMed id: 7520819

Structure of a soluble, glycosylated form of the human complement regulatory protein CD59.

C.M.Fletcher, R.A.Harrison, P.J.Lachmann, D.Neuhaus.

ABSTRACT

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.

Selected figure(s)

Figure 9.
Figure 9. Distribution of the χ^2 angles of Asn18 in the two sets of structures for which oligosaccharide fragments were included in the computational model. Figure 9. Distribution of the χ^2 angles of Asn18 in the two sets of structures for which oligosaccharide fragments were included in the computational model.

Figure 11.
Figure 11. Amino acid sequences of CD59 and homologous proteins. Residue numbers refer to the human CD59 sequence; amino acids which are conserved with human CD59 are shown in red. For sheep and rat CD59, only partial sequences are available and ‘x’ indicates a residue which was not identified during protein sequencing. For HVS-15, the amino- and carboxy-terminal residues of the mature protein are not known but are based on the predicted leader peptide [4] and comparison with human CD59 [1, 2, 3, 5, 54, 55, 56, 57, 58, 59 and 60]. Figure 11. Amino acid sequences of CD59 and homologous proteins. Residue numbers refer to the human CD59 sequence; amino acids which are conserved with human CD59 are shown in red. For sheep and rat CD59, only partial sequences are available and ‘x’ indicates a residue which was not identified during protein sequencing. For HVS-15, the amino- and carboxy-terminal residues of the mature protein are not known but are based on the predicted leader peptide [[3]4] and comparison with human CD59 [[4]1, [5]2, [6]3, [7]5, [8]54, [9]55, [10]56, [11]57, [12]58, [13]59 and [14]60].

The above figures are reprinted by permission from Cell Press: Structure (1994, 2, 185-199) copyright 1994.

Figures were selected by an automated process.