PDBsum entry: 1cr8

Lipid binding protein

PDB-id

1cr8


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PDB id:

1cr8

Name:

Lipid binding protein

Title:

Low density lipoprotein receptor-related protein complement repeat 8

Structure:

Protein (low density lipoprotein receptor related protein). Chain: a. Fragment: complement repeat 8. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Organ: liver, placenta. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: bl21.

UniProt:

Q07954 (LRP1_HUMAN)

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4544 a.a.

Struc:

42 a.a.

Key:		PfamA domain
		Secondary structure			CATH domain

Resolution:

not givenÅ

NMR structure:

20 models

Authors:

W.Huang,K.Dolmer,P.G.W.Gettins

Key ref:

W.Huang et al. (1999). NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein.. J Biol Chem, 274, 14130-14136. [PubMed id: 10318830] [DOI: 10.1074/jbc.274.20.14130]

Date:

14-Dec-98

Release date:

23-Dec-98

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Key reference

DOI no: 10.1074/jbc.274.20.14130 J Biol Chem 274:14130-14136 (1999)

PubMed id: 10318830

NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein.

W.Huang, K.Dolmer, P.G.Gettins.

ABSTRACT

The low density lipoprotein receptor-related protein is a member of the low density lipoprotein receptor family and contains clusters of cysteine-rich complement-like repeats of about 42 residues that are present in all members of this family of receptors. These clusters are thought to be the principal binding sites for protein ligands. We have expressed one complement-like repeat, CR8, from the cluster in lipoprotein receptor-related protein that binds certain proteinase inhibitor-proteinase complexes and used three-dimensional NMR on the 13C/15N-labeled protein to determine the structure in solution of the calcium-bound form. The structure is very similar in overall fold to repeat 5 from the low density lipoprotein receptor (LB5), with backbone root mean square deviation of 1.5 A. The calcium-binding site also appears to be homologous, with four carboxyl and two backbone carbonyl ligands. However, differences in primary structure are such that equivalent surfaces that might represent the binding interfaces are very different from one another, indicating that different domains will have very different ligand specificities.

Selected figure(s)

Figure 6.
Fig. 6. Comparison of the calcium coordination sites of CR8 and LB5. The views are the same as that in Fig. 5. The coordinates for the LB5 representation were obtained from Brookhaven Protein Data Bank, from deposition 1ajj. Because the coordinates of Ca^2+ are not provided in 1ajj, the position was inferred from the published ligand-calcium separations. Figure 7.
Fig. 7. Structural comparison of the backbones of CR8 (dark line) and LB5 (light line) using deposited coordinates of LB5 and the lowest energy NMR structure of CR8 from those depicted in Fig. 4. Statistics for the comparison are presented in Table II. A, best overlay of the whole structures. B, best overlay of the N-terminal -sheet-containing region. C, best overlay of the calcium-binding region.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (1999, 274, 14130-14136) copyright 1999.

Figures were selected by an automated process.

Literature references that cite this PDB file's key reference

PubMed id Reference

18331356 S.D.Roosendaal, J.Kerver, M.Schipper, K.W.Rodenburg, and D.J.Van der Horst (2008).
The complex of the insect LDL receptor homolog, lipophorin receptor, LpR, and its lipoprotein ligand does not dissociate under endosomal conditions.

FEBS J, 275, 1751-1766.

17245526 C.A.Wolf, F.Dancea, M.Shi, V.Bade-Noskova, H.Rüterjans, D.Kerjaschki, and C.Lücke (2007).
Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin.

J Biomol NMR, 37, 321-328.

PDB code: 2i1p

15952897 H.Jeon, and S.C.Blacklow (2005).
Structure and physiologic function of the low-density lipoprotein receptor.

Annu Rev Biochem, 74, 535-562.

16299519 J.Silverman, Q.Liu, Q.Lu, A.Bakker, W.To, A.Duguay, B.M.Alba, R.Smith, A.Rivas, P.Li, H.Le, E.Whitehorn, K.W.Moore, C.Swimmer, V.Perlroth, M.Vogt, J.Kolkman, and W.P.Stemmer (2005).
Multivalent avimer proteins evolved by exon shuffling of a family of human receptor domains.

Nat Biotechnol, 23, 1556-1561.

15064754 N.Verdaguer, I.Fita, M.Reithmayer, R.Moser, and D.Blaas (2004).
X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein.

Nat Struct Mol Biol, 11, 429-434.

PDB code: 1v9u

14694099 T.Rai, D.Marble, K.Rihani, and L.Rong (2004).
The spacing between cysteines two and three of the LDL-A module of Tva is important for subgroup A avian sarcoma and leukosis virus entry.

J Virol, 78, 683-691.

12381843 Q.Y.Wang, B.Manicassamy, X.Yu, K.Dolmer, P.G.Gettins, and L.Rong (2002).
Characterization of the LDL-A module mutants of Tva, the subgroup A Rous sarcoma virus receptor, and the implications in protein folding.

Protein Sci, 11, 2596-2605.

11861852 Q.Y.Wang, W.Huang, K.Dolmer, P.G.Gettins, and L.Rong (2002).
Solution structure of the viral receptor domain of Tva and its implications in viral entry.

J Virol, 76, 2848-2856.

PDB code: 1jrf

11560943 J.Herz, and D.K.Strickland (2001).
LRP: a multifunctional scavenger and signaling receptor.

J Clin Invest, 108, 779-784.

11258891 N.Beglova, C.L.North, and S.C.Blacklow (2001).
Backbone dynamics of a module pair from the ligand-binding domain of the LDL receptor.

Biochemistry, 40, 2808-2815.

11160709 Q.Y.Wang, K.Dolmer, W.Huang, P.G.Gettins, and L.Rong (2001).
Role of calcium in protein folding and function of Tva, the receptor of subgroup A avian sarcoma and leukosis virus.

J Virol, 75, 2051-2058.

10704205 C.L.North, and S.C.Blacklow (2000).
Solution structure of the sixth LDL-A module of the LDL receptor.

Biochemistry, 39, 2564-2571.

PDB code: 1d2j

11101504 E.A.Hewat, E.Neumann, J.F.Conway, R.Moser, B.Ronacher, T.C.Marlovits, and D.Blaas (2000).
The cellular receptor to human rhinovirus 2 binds around the 5-fold axis and not in the canyon: a structural view.

EMBO J, 19, 6317-6325.

10933493 N.D.Kurniawan, A.R.Atkins, S.Bieri, C.J.Brown, I.M.Brereton, P.A.Kroon, and R.Smith (2000).
NMR structure of a concatemer of the first and second ligand-binding modules of the human low-density lipoprotein receptor.

Protein Sci, 9, 1282-1293.

PDB code: 1f5y

10978145 O.M.Andersen, P.A.Christensen, L.L.Christensen, C.Jacobsen, S.K.Moestrup, M.Etzerodt, and H.C.Thogersen (2000).
Specific binding of alpha-macroglobulin to complement-type repeat CR4 of the low-density lipoprotein receptor-related protein.

Biochemistry, 39, 10627-10633.

11106161 T.Xiao, D.L.DeCamp, and S.R.Spran (2000).
Structure of a rat alpha 1-macroglobulin receptor-binding domain dimer.

Protein Sci, 9, 1889-1897.

PDB code: 1edy

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.