2R2O
Crystal structure of the effector domain of human Plexin B1
Summary for 2R2O
Entry DOI | 10.2210/pdb2r2o/pdb |
Descriptor | Plexin-B1, UNKNOWN ATOM OR ION (3 entities in total) |
Functional Keywords | plexin, effector domain, structural genomics, structural genomics consortium, sgc, glycoprotein, membrane, phosphorylation, receptor, secreted, transmembrane, signaling protein |
Biological source | Homo sapiens (human) |
Cellular location | Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted. Isoform 3: Secreted: O43157 |
Total number of polymer chains | 2 |
Total formula weight | 31068.52 |
Authors | Tong, Y.,Tempel, W.,Shen, L.,Arrowsmith, C.H.,Edwards, A.M.,Sundstrom, M.,Weigelt, J.,Bochkarev, A.,Park, H.,Structural Genomics Consortium (SGC) (deposition date: 2007-08-27, release date: 2007-09-04, Last modification date: 2017-10-25) |
Primary citation | Tong, Y.,Chugha, P.,Hota, P.K.,Alviani, R.S.,Li, M.,Tempel, W.,Shen, L.,Park, H.W.,Buck, M. Binding of Rac1, Rnd1, and RhoD to a novel Rho GTPase interaction motif destabilizes dimerization of the plexin-B1 effector domain. J.Biol.Chem., 282:37215-37224, 2007 Cited by PubMed: 17916560DOI: 10.1074/jbc.M703800200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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