1m9z

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(New page: 200px<br /> <applet load="1m9z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m9z, resolution 1.05&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1m9z.gif|left|200px]]<br />
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[[Image:1m9z.gif|left|200px]]<br /><applet load="1m9z" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1m9z" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1m9z, resolution 1.05&Aring;" />
caption="1m9z, resolution 1.05&Aring;" />
'''CRYSTAL STRUCTURE OF HUMAN TGF-BETA TYPE II RECEPTOR LIGAND BINDING DOMAIN'''<br />
'''CRYSTAL STRUCTURE OF HUMAN TGF-BETA TYPE II RECEPTOR LIGAND BINDING DOMAIN'''<br />
==Overview==
==Overview==
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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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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.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1M9Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M9Z OCA].
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1M9Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M9Z OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Boesen, C.C.]]
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[[Category: Boesen, C C.]]
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[[Category: Motyka, S.A.]]
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[[Category: Motyka, S A.]]
[[Category: Patamawenu, A.]]
[[Category: Patamawenu, A.]]
[[Category: Radaev, S.]]
[[Category: Radaev, S.]]
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[[Category: Sun, P.D.]]
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[[Category: Sun, P D.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: three finger toxin fold]]
[[Category: three finger toxin fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:09:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:53:04 2008''

Revision as of 11:53, 21 February 2008


1m9z, resolution 1.05Å

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

Contents

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.

Disease

Known diseases associated with this structure: Aortic aneurysm, familial thoracic 3 OMIM:[190182], Colon cancer OMIM:[190182], Colorectal cancer, hereditary nonpolyposis, type 6 OMIM:[190182], Esophageal cancer OMIM:[190182], Loeys-Dietz syndrome OMIM:[190182], Marfan syndrome, type II OMIM:[190182]

About this Structure

1M9Z is a Single protein structure of sequence from Homo sapiens with as ligand. 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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