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1KI1

Guanine Nucleotide Exchange Region of Intersectin in Complex with Cdc42

Summary for 1KI1
Entry DOI10.2210/pdb1ki1/pdb
DescriptorG25K GTP-binding protein, placental isoform, intersectin long form, SULFATE ION, ... (4 entities in total)
Functional Keywordsprotein-protein complex, dh domain, ph domain, rho gtpase, signaling protein
Biological sourceHomo sapiens (human)
More
Cellular locationCell membrane; Lipid-anchor; Cytoplasmic side (Potential): P60953
Endomembrane system (By similarity): Q15811
Total number of polymer chains4
Total formula weight123949.31
Authors
Snyder, J.T.,Pruitt, W.M.,Der, C.J.,Sondek, J. (deposition date: 2001-12-02, release date: 2002-05-29, Last modification date: 2024-02-14)
Primary citationSnyder, J.T.,Worthylake, D.K.,Rossman, K.L.,Betts, L.,Pruitt, W.M.,Siderovski, D.P.,Der, C.J.,Sondek, J.
Structural basis for the selective activation of Rho GTPases by Dbl exchange factors.
Nat.Struct.Biol., 9:468-475, 2002
Cited by
PubMed Abstract: 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.
PubMed: 12006984
DOI: 10.1038/nsb796
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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