1RJ2

Crystal structure of the DH/PH fragment of Dbs without bound GTPase

Summary for 1RJ2

• Entry DOI: 10.2210/pdb1rj2/pdb
• Related: 1FOE 1KZ7 1KZG 1LB1
• Descriptor: Guanine nucleotide exchange factor DBS [Fragment] (2 entities in total)
• Functional Keywords: dbl homology; pleckstrin homology; guanine nucleotide exchange factor; rho gtpase, signaling protein
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm: Q63406
• Total number of polymer chains: 4
• Total formula weight: 164881.33

Authors

Worthylake, D.K.,Rossman, K.L.,Sondek, J. (deposition date: 2003-11-18, release date: 2004-06-29, Last modification date: 2023-08-23)

Primary citation

Worthylake, D.K.,Rossman, K.L.,Sondek, J.
Crystal structure of the DH/PH fragment of Dbs without bound GTPase.
Structure, 12:1078-1086, 2004

PubMed Abstract: Dbl proteins are guanine nucleotide exchange factors for Rho GTPases, containing adjacent Dbl homology (DH) and pleckstrin homology (PH) domains. This domain architecture is virtually invariant and typically required for full exchange potential. Several structures of DH/PH fragments bound to GTPases implicate the PH domain in nucleotide exchange. To more fully understand the functional linkage between DH and PH domains, we have determined the crystal structure of the DH/PH fragment of Dbs without bound GTPase. This structure is generally similar to previously determined structures of Dbs bound to GTPases albeit with greater apparent mobility between the DH and PH domains. These comparisons suggest that the DH and PH domains of Dbs are spatially primed for binding GTPases and small alterations in intradomain conformations that may be elicited by subtle biological responses, such as altered phosphoinositide levels, are sufficient to enhance exchange by facilitating interactions between the PH domain and GTPases.

PubMed: 15274927
DOI: 10.1016/j.str.2004.03.021

Experimental method

X-RAY DIFFRACTION (3 Å)