1m9z

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|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1ktz|1KTZ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m9z OCA], [http://www.ebi.ac.uk/pdbsum/1m9z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m9z RCSB]</span>
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==Overview==
==Overview==
Transforming growth factor beta (TGF-beta) is involved in a wide range of biological functions including development, carcinogenesis, and immune regulation. Here we report the 1.1 A resolution crystal structure of human TGF-beta type II receptor ectodomain (TBRII). The overall structure of TBRII is similar to that of activin type II receptor ectodomain (ActRII) and bone morphogenic protein receptor type IA (BRIA). It displays a three-finger toxin fold with fingers formed by the beta strand pairs beta1-beta2, beta3-beta4, and beta5-beta6. The first finger in the TBRII is significantly longer than in ActRII and BRIA and folds tightly between the second finger and the C terminus. Surface charge distributions and hydrophobic patches predict potential TBRII binding sites.
Transforming growth factor beta (TGF-beta) is involved in a wide range of biological functions including development, carcinogenesis, and immune regulation. Here we report the 1.1 A resolution crystal structure of human TGF-beta type II receptor ectodomain (TBRII). The overall structure of TBRII is similar to that of activin type II receptor ectodomain (ActRII) and bone morphogenic protein receptor type IA (BRIA). It displays a three-finger toxin fold with fingers formed by the beta strand pairs beta1-beta2, beta3-beta4, and beta5-beta6. The first finger in the TBRII is significantly longer than in ActRII and BRIA and folds tightly between the second finger and the C terminus. Surface charge distributions and hydrophobic patches predict potential TBRII binding sites.
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==Disease==
 
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Known diseases associated with this structure: Colorectal cancer, hereditary nonpolyposis, type 6 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=190182 190182]], Esophageal cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=190182 190182]], Loeys-Dietz syndrome, type 1B OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=190182 190182]], Loeys-Dietz syndrome, type 2B OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=190182 190182]]
 
==About this Structure==
==About this Structure==
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[[Category: Radaev, S.]]
[[Category: Radaev, S.]]
[[Category: Sun, P D.]]
[[Category: Sun, P D.]]
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[[Category: GOL]]
 
[[Category: three finger toxin fold]]
[[Category: three finger toxin fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:40:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:13:20 2008''

Revision as of 19:13, 30 March 2008


PDB ID 1m9z

Drag the structure with the mouse to rotate
, resolution 1.05Å
Ligands:
Related: 1KTZ


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF HUMAN TGF-BETA TYPE II RECEPTOR LIGAND BINDING DOMAIN


Overview

Transforming growth factor beta (TGF-beta) is involved in a wide range of biological functions including development, carcinogenesis, and immune regulation. Here we report the 1.1 A resolution crystal structure of human TGF-beta type II receptor ectodomain (TBRII). The overall structure of TBRII is similar to that of activin type II receptor ectodomain (ActRII) and bone morphogenic protein receptor type IA (BRIA). It displays a three-finger toxin fold with fingers formed by the beta strand pairs beta1-beta2, beta3-beta4, and beta5-beta6. The first finger in the TBRII is significantly longer than in ActRII and BRIA and folds tightly between the second finger and the C terminus. Surface charge distributions and hydrophobic patches predict potential TBRII binding sites.

About this Structure

1M9Z is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The 1.1 A crystal structure of human TGF-beta type II receptor ligand binding domain., Boesen CC, Radaev S, Motyka SA, Patamawenu A, Sun PD, Structure. 2002 Jul;10(7):913-9. PMID:12121646

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