1dbh: Difference between revisions

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[[Image:1dbh.~~gif~~|left|200px]]

[[Image:1dbh.png|left|200px]]

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~~'''~~DBL AND PLECKSTRIN HOMOLOGY DOMAINS FROM HSOS1~~'''~~

===DBL AND PLECKSTRIN HOMOLOGY DOMAINS FROM HSOS1===

~~==Overview==~~

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~~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.

The line below this paragraph, {{ABSTRACT_PUBMED_9790532}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9790532 is the PubMed ID number.

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==About this Structure==

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[[Category: Soisson, S M.]]

[[Category: Guanine nucleotide exchange factor]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 13~~:39:32 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:46:44 2008''

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-[[Image:1dbh.gif|left|200px]]
+{{Seed}}
+[[Image:1dbh.png|left|200px]]
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 {{STRUCTURE_1dbh|  PDB=1dbh  |  SCENE=  }}
-'''DBL AND PLECKSTRIN HOMOLOGY DOMAINS FROM HSOS1'''
+===DBL AND PLECKSTRIN HOMOLOGY DOMAINS FROM HSOS1===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9790532}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9790532 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9790532}}
 ==About this Structure==
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 [[Category: Soisson, S M.]]
 [[Category: Guanine nucleotide exchange factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:39:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:46:44 2008''