1ayo
From Proteopedia
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| - | [[Image:1ayo.gif|left|200px]] | + | [[Image:1ayo.gif|left|200px]] |
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| - | '''RECEPTOR BINDING DOMAIN OF BOVINE ALPHA-2-MACROGLOBULIN''' | + | {{Structure |
| + | |PDB= 1ayo |SIZE=350|CAPTION= <scene name='initialview01'>1ayo</scene>, resolution 1.90Å | ||
| + | |SITE= <scene name='pdbsite=S1:N-Linked+Glycosylation+Site'>S1</scene> and <scene name='pdbsite=S2:N-Linked+Glycosylation+Site'>S2</scene> | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''RECEPTOR BINDING DOMAIN OF BOVINE ALPHA-2-MACROGLOBULIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AYO is a [ | + | 1AYO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AYO OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9634697 9634697] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: receptor binding domain]] | [[Category: receptor binding domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:03:57 2008'' |
Revision as of 08:03, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Sites: | and | ||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
RECEPTOR BINDING DOMAIN OF BOVINE ALPHA-2-MACROGLOBULIN
Contents |
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.
Disease
Known diseases associated with this structure: Alzheimer disease, susceptibility to OMIM:[103950], Emphysema due to alpha-2-macroglobulin deficiency OMIM:[103950]
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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