1dbh: Difference between revisions

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New page: left|200px<br /> <applet load="1dbh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dbh, resolution 2.3Å" /> '''DBL AND PLECKSTRIN H...
 
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[[Image:1dbh.gif|left|200px]]<br />
[[Image:1dbh.gif|left|200px]]<br /><applet load="1dbh" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1dbh" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1dbh, resolution 2.3&Aring;" />
caption="1dbh, resolution 2.3&Aring;" />
'''DBL AND PLECKSTRIN HOMOLOGY DOMAINS FROM HSOS1'''<br />
'''DBL AND PLECKSTRIN HOMOLOGY DOMAINS FROM HSOS1'''<br />


==Overview==
==Overview==
Proteins containing Dbl homology (DH) domains activate Rho-family GTPases, by functioning as specific guanine nucleotide exchange factors. All known, DH domains have associated C-terminal pleckstrin homology (PH) domains, that are implicated in targeting and regulatory functions. The crystal, structure of a fragment of the human Son of sevenless protein containing, the DH and PH domains has been determined at 2.3 A resolution. The, entirely alpha-helical DH domain is unrelated in architecture to other, nucleotide exchange factors. The active site of the DH domain, identified, on the basis of sequence conservation and structural features, lies near, the interface between the DH and PH domains. The structure suggests that, ligation of the PH domain will be coupled structurally to the GTPase, binding site.
Proteins containing Dbl homology (DH) domains activate Rho-family GTPases by functioning as specific guanine nucleotide exchange factors. All known DH domains have associated C-terminal pleckstrin homology (PH) domains that are implicated in targeting and regulatory functions. The crystal structure of a fragment of the human Son of sevenless protein containing the DH and PH domains has been determined at 2.3 A resolution. The entirely alpha-helical DH domain is unrelated in architecture to other nucleotide exchange factors. The active site of the DH domain, identified on the basis of sequence conservation and structural features, lies near the interface between the DH and PH domains. The structure suggests that ligation of the PH domain will be coupled structurally to the GTPase binding site.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1DBH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DBH OCA].  
1DBH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DBH OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Kuriyan, J.]]
[[Category: Kuriyan, J.]]
[[Category: Soisson, S.M.]]
[[Category: Soisson, S M.]]
[[Category: guanine nucleotide exchange factor]]
[[Category: guanine nucleotide exchange factor]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:14:53 2008''

Revision as of 13:14, 21 February 2008

File:1dbh.gif


1dbh, resolution 2.3Å

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DBL AND PLECKSTRIN HOMOLOGY DOMAINS FROM HSOS1

OverviewOverview

Proteins containing Dbl homology (DH) domains activate Rho-family GTPases by functioning as specific guanine nucleotide exchange factors. All known DH domains have associated C-terminal pleckstrin homology (PH) domains that are implicated in targeting and regulatory functions. The crystal structure of a fragment of the human Son of sevenless protein containing the DH and PH domains has been determined at 2.3 A resolution. The entirely alpha-helical DH domain is unrelated in architecture to other nucleotide exchange factors. The active site of the DH domain, identified on the basis of sequence conservation and structural features, lies near the interface between the DH and PH domains. The structure suggests that ligation of the PH domain will be coupled structurally to the GTPase binding site.

DiseaseDisease

Known diseases associated with this structure: Fibromatosis, gingival OMIM:[182530], Noonan syndrome 4 OMIM:[182530]

About this StructureAbout this Structure

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

ReferenceReference

Crystal structure of the Dbl and pleckstrin homology domains from the human Son of sevenless protein., Soisson SM, Nimnual AS, Uy M, Bar-Sagi D, Kuriyan J, Cell. 1998 Oct 16;95(2):259-68. PMID:9790532

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