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1ayo

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|PDB= 1ayo |SIZE=350|CAPTION= <scene name='initialview01'>1ayo</scene>, resolution 1.90&Aring;
|PDB= 1ayo |SIZE=350|CAPTION= <scene name='initialview01'>1ayo</scene>, resolution 1.90&Aring;
|SITE= <scene name='pdbsite=S1:N-Linked+Glycosylation+Site'>S1</scene> and <scene name='pdbsite=S2:N-Linked+Glycosylation+Site'>S2</scene>
|SITE= <scene name='pdbsite=S1:N-Linked+Glycosylation+Site'>S1</scene> and <scene name='pdbsite=S2:N-Linked+Glycosylation+Site'>S2</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ayo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ayo OCA], [http://www.ebi.ac.uk/pdbsum/1ayo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ayo RCSB]</span>
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}}
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==Overview==
==Overview==
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.
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.
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==Disease==
 
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Known diseases associated with this structure: Alzheimer disease, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=103950 103950]], Emphysema due to alpha-2-macroglobulin deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=103950 103950]]
 
==About this Structure==
==About this Structure==
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[[Category: Sottrup-Jensen, L.]]
[[Category: Sottrup-Jensen, L.]]
[[Category: Thirup, S.]]
[[Category: Thirup, S.]]
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[[Category: CA]]
 
[[Category: macroglobulin]]
[[Category: macroglobulin]]
[[Category: receptor binding domain]]
[[Category: receptor binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:03:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:50:06 2008''

Revision as of 15:50, 30 March 2008

Image:1ayo.gif


PDB ID 1ayo

Drag the structure with the mouse to rotate
, resolution 1.90Å
Sites: and
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



RECEPTOR BINDING DOMAIN OF BOVINE ALPHA-2-MACROGLOBULIN


Overview

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.

About this Structure

1AYO is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the receptor-binding domain of alpha 2-macroglobulin., Jenner L, Husted L, Thirup S, Sottrup-Jensen L, Nyborg J, Structure. 1998 May 15;6(5):595-604. PMID:9634697

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