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PDBsum entry 1bv8
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Protein binding PDB id
1bv8

 

 

 

 

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Contents
Protein chain
138 a.a. *
* Residue conservation analysis
PDB id:
1bv8
Name: Protein binding
Title: Receptor domain from alpha-2-macroglobulin
Structure: Alpha-2-macroglobulin. Chain: a. Fragment: receptor binding domain. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: bl21.
NMR struc: 1 models
Authors: W.Huang,K.Dolmer,X.Liao,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:
22-Sep-98     Release date:   05-Apr-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01023  (A2MG_HUMAN) -  Alpha-2-macroglobulin from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1474 a.a.
138 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
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
21054788 K.Duus, N.M.Thielens, M.Lacroix, P.Tacnet, P.Frachet, U.Holmskov, and G.Houen (2010).
CD91 interacts with mannan-binding lectin (MBL) through the MBL-associated serine protease-binding site.
  FEBS J, 277, 4956-4964.  
20030366 M.Guttman, J.H.Prieto, J.E.Croy, and E.A.Komives (2010).
Decoding of lipoprotein-receptor interactions: properties of ligand binding modules governing interactions with apolipoprotein E.
  Biochemistry, 49, 1207-1216.  
20303980 M.Guttman, J.H.Prieto, T.M.Handel, P.J.Domaille, and E.A.Komives (2010).
Structure of the minimal interface between ApoE and LRP.
  J Mol Biol, 398, 306-319.
PDB codes: 2knx 2kny
19439404 J.K.Jensen, K.Dolmer, and P.G.Gettins (2009).
Specificity of binding of the low density lipoprotein receptor-related protein to different conformational states of the clade E serpins plasminogen activator inhibitor-1 and proteinase nexin-1.
  J Biol Chem, 284, 17989-17997.  
  18626063 A.P.Lillis, L.B.Van Duyn, J.E.Murphy-Ullrich, and D.K.Strickland (2008).
LDL receptor-related protein 1: unique tissue-specific functions revealed by selective gene knockout studies.
  Physiol Rev, 88, 887-918.  
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
16814863 C.S.Samuel, X.J.Du, R.A.Bathgate, and R.J.Summers (2006).
'Relaxin' the stiffened heart and arteries: the therapeutic potential for relaxin in the treatment of cardiovascular disease.
  Pharmacol Ther, 112, 529-552.  
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.  
15950875 N.Beglova, and S.C.Blacklow (2005).
The LDL receptor: how acid pulls the trigger.
  Trends Biochem Sci, 30, 309-317.  
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 codes are shown on the right.

 

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