1lb1

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{{STRUCTURE_1lb1| PDB=1lb1 | SCENE= }}
{{STRUCTURE_1lb1| PDB=1lb1 | SCENE= }}
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'''Crystal Structure of the Dbl and Pleckstrin homology domains of Dbs in complex with RhoA'''
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===Crystal Structure of the Dbl and Pleckstrin homology domains of Dbs in complex with RhoA===
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==Overview==
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Activation of Rho-family GTPases involves the removal of bound GDP and the subsequent loading of GTP, all catalyzed by guanine nucleotide exchange factors (GEFs) of the Dbl-family. Despite high sequence conservation among Rho GTPases, Dbl proteins possess a wide spectrum of discriminatory potentials for Rho-family members. To rationalize this specificity, we have determined crystal structures of the conserved, catalytic fragments (Dbl and pleckstrin homology domains) of the exchange factors intersectin and Dbs in complex with their cognate GTPases, Cdc42 and RhoA, respectively. Structure-based mutagenesis of intersectin and Dbs reveals the key determinants responsible for promoting exchange activity in Cdc42, Rac1 and RhoA. These findings provide critical insight into the structural features necessary for the proper pairing of Dbl-exchange factors with Rho GTPases and now allow for the detailed manipulation of signaling pathways mediated by these oncoproteins in vivo.
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{{ABSTRACT_PUBMED_12006984}}
==About this Structure==
==About this Structure==
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[[Category: Rhoa]]
[[Category: Rhoa]]
[[Category: Small g-protein]]
[[Category: Small g-protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:44:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 12:11:03 2008''

Revision as of 09:11, 2 July 2008

Template:STRUCTURE 1lb1

Crystal Structure of the Dbl and Pleckstrin homology domains of Dbs in complex with RhoA

Template:ABSTRACT PUBMED 12006984

About this Structure

1LB1 is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural basis for the selective activation of Rho GTPases by Dbl exchange factors., Snyder JT, Worthylake DK, Rossman KL, Betts L, Pruitt WM, Siderovski DP, Der CJ, Sondek J, Nat Struct Biol. 2002 Jun;9(6):468-75. PMID:12006984

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