We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1ayo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==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.
==Disease==
==Disease==
Line 17: Line 17:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Husted, L.]]
[[Category: Husted, L.]]
-
[[Category: Jenner, L.B.]]
+
[[Category: Jenner, L B.]]
[[Category: Nyborg, J.]]
[[Category: Nyborg, J.]]
[[Category: Sottrup-Jensen, L.]]
[[Category: Sottrup-Jensen, L.]]
Line 25: Line 25:
[[Category: receptor binding domain]]
[[Category: receptor binding domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:32:10 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:49:39 2008''

Revision as of 09:49, 21 February 2008

Image:1ayo.gif

1ayo, resolution 1.90Å

Drag the structure with the mouse to rotate

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 with as ligand. Known structural/functional Sites: and . 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

Page seeded by OCA on Thu Feb 21 11:49:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ayo"
Personal tools