PDBsum entry 1ayo

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Macroglobulin PDB id
Protein chains
130 a.a. *
Waters ×304
* Residue conservation analysis
PDB id:
Name: Macroglobulin
Title: Receptor binding domain of bovine alpha-2-macroglobulin
Structure: Alpha-2-macroglobulin. Chain: a, b. Fragment: receptor-binding domain. Other_details: n-linked glycosylation site on asn b 68
Source: Bos taurus. Cattle. Organism_taxid: 9913. Tissue: plasma
Biol. unit: Tetramer (from PQS)
1.90Å     R-factor:   0.197     R-free:   0.239
Authors: L.B.Jenner,L.Husted,S.Thirup,L.Sottrup-Jensen,J.Nyborg
Key ref:
L.Jenner et al. (1998). Crystal structure of the receptor-binding domain of alpha 2-macroglobulin. Structure, 6, 595-604. PubMed id: 9634697 DOI: 10.1016/S0969-2126(98)00061-6
07-Nov-97     Release date:   25-Nov-98    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q7SIH1  (A2MG_BOVIN) -  Alpha-2-macroglobulin
1510 a.a.
130 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 


DOI no: 10.1016/S0969-2126(98)00061-6 Structure 6:595-604 (1998)
PubMed id: 9634697  
Crystal structure of the receptor-binding domain of alpha 2-macroglobulin.
L.Jenner, L.Husted, S.Thirup, L.Sottrup-Jensen, J.Nyborg.
BACKGROUND: The large plasma proteinase inhibitors of the alpha 2-macroglobulin superfamily inhibit proteinases by capturing them within a central cavity of the inhibitor molecule. After reaction with the proteinase, the alpha-macroglobulin-proteinase complex binds to the alpha-macroglobulin receptor, present in the liver and other tissues, and becomes endocytosed and rapidly removed from the circulation. The complex binds to the receptor via recognition sites located on a separate domain of approximately 138 residues positioned at the C terminus of the alpha-macroglobulin subunit. RESULTS: The crystal structure of the receptor-binding domain of bovine alpha 2-macroglobulin (bRBD) has been determined at a resolution of 1.9 A. The domain primarily comprises a nine-strand beta structure with a jelly-roll topology, but also contains two small alpha helices. CONCLUSIONS: The surface patch responsible for receptor recognition is thought to involve residues located on one of the two alpha helices of the bRBD as well as residues in two of the beta strands. Located on this alpha helix are two lysine residues that are important for receptor binding. The structure of bRBD is very similar to the approximately 100-residue C-terminal domain of factor XIII, a transglutaminase from the blood coagulation system.
  Selected figure(s)  
Figure 5.
Figure 5. Stereoview showing a superposition of bRBD and the C-terminal domain of factor XIII. bRBD is shown in blue and factor XIII is in grey. The b-a-b motif is located at the top of the b sandwiches in this view, and is missing in factor XIII. (The figure was prepared with the program MOLSCRIPT [66].)
  The above figure is reprinted by permission from Cell Press: Structure (1998, 6, 595-604) copyright 1998.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19368894 V.Krishnan, K.Ponnuraj, Y.Xu, K.Macon, J.E.Volanakis, and S.V.Narayana (2009).
The crystal structure of cobra venom factor, a cofactor for C3- and C5-convertase CVFBb.
  Structure, 17, 611-619.
PDB code: 3frp
18800165 Y.Yoshiike, R.Minai, Y.Matsuo, Y.R.Chen, T.Kimura, and A.Takashima (2008).
Amyloid oligomer conformation in a group of natively folded proteins.
  PLoS ONE, 3, e3235.  
17603498 K.D.Corbett, P.Benedetti, and J.M.Berger (2007).
Holoenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VI.
  Nat Struct Mol Biol, 14, 611-619.
PDB code: 2q2e
16641085 S.Arandjelovic, C.L.Van Sant, and S.L.Gonias (2006).
Limited mutations in full-length tetrameric human alpha2-macroglobulin abrogate binding of platelet-derived growth factor-BB and transforming growth factor-beta1.
  J Biol Chem, 281, 17061-17068.  
16177781 B.J.Janssen, E.G.Huizinga, H.C.Raaijmakers, A.Roos, M.R.Daha, K.Nilsson-Ekdahl, B.Nilsson, and P.Gros (2005).
Structures of complement component C3 provide insights into the function and evolution of immunity.
  Nature, 437, 505-511.
PDB codes: 2a73 2a74
15773905 J.M.Mettenburg, S.Arandjelovic, and S.L.Gonias (2005).
A chemically modified preparation of alpha2-macroglobulin binds beta-amyloid peptide with increased affinity and inhibits Abeta cytotoxicity.
  J Neurochem, 93, 53-62.  
15611997 V.K.Lin, S.Y.Wang, N.C.Boetticher, D.V.Vazquez, H.Saboorian, J.D.McConnell, and C.G.Roehrborn (2005).
Alpha(2) macroglobulin, a PSA binding protein, is expressed in human prostate stroma.
  Prostate, 63, 299-308.  
15194799 F.Gaden, L.Franqueville, M.K.Magnusson, S.S.Hong, M.D.Merten, L.Lindholm, and P.Boulanger (2004).
Gene transduction and cell entry pathway of fiber-modified adenovirus type 5 vectors carrying novel endocytic peptide ligands selected on human tracheal glandular cells.
  J Virol, 78, 7227-7247.  
12485987 C.C.Deivanayagam, E.R.Wann, W.Chen, M.Carson, K.R.Rajashankar, M.Höök, and S.V.Narayana (2002).
A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A.
  EMBO J, 21, 6660-6672.
PDB code: 1n67
11823454 J.M.Mettenburg, D.J.Webb, and S.L.Gonias (2002).
Distinct binding sites in the structure of alpha 2-macroglobulin mediate the interaction with beta-amyloid peptide and growth factors.
  J Biol Chem, 277, 13338-13345.  
12218066 L.B.Husted, E.S.Sorensen, P.B.Armstrong, J.P.Quigley, L.Kristensen, and L.Sottrup-Jensen (2002).
Localization of carbohydrate attachment sites and disulfide bridges in limulus alpha 2-macroglobulin. Evidence for two forms differing primarily in their bait region sequences.
  J Biol Chem, 277, 43698-43706.  
12234368 M.A.Arnaout (2002).
Integrin structure: new twists and turns in dynamic cell adhesion.
  Immunol Rev, 186, 125-140.  
10652313 K.Dolmer, W.Huang, and P.G.Gettins (2000).
NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin.
  J Biol Chem, 275, 3264-3269.
PDB code: 1d2l
10866810 M.Gunnarsson, T.Stigbrand, and P.E.Jensen (2000).
Conformational variants of human alpha2-macroglobulin are reflected in a C-terminal 'switch region'.
  Eur J Biochem, 267, 4081-4087.  
  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
10625650 W.Huang, K.Dolmer, X.Liao, and P.G.Gettins (2000).
NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin.
  J Biol Chem, 275, 1089-1094.  
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.