2C7N
Human Rabex-5 residues 1-74 in complex with Ubiquitin
Summary for 2C7N
Entry DOI | 10.2210/pdb2c7n/pdb |
Related | 1AAR 1E0Q 1P3Q 1UZX 1V80 1V81 1WR6 1WRD 1YD8 2BGF 2C7M |
Descriptor | RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1, UBIQUITIN, ZINC ION, ... (4 entities in total) |
Functional Keywords | protein-binding, ubiquitin binding domain, endocytosis, nuclear protein, polyprotein, ubiquitin complex, protein binding |
Biological source | HOMO SAPIENS (HUMAN) More |
Total number of polymer chains | 12 |
Total formula weight | 104562.01 |
Authors | Penengo, L.,Mapelli, M.,Murachelli, A.G.,Confalioneri, S.,Magri, L.,Musacchio, A.,Di Fiore, P.P.,Polo, S.,Schneider, T.R. (deposition date: 2005-11-25, release date: 2006-02-15, Last modification date: 2024-05-08) |
Primary citation | Penengo, L.,Mapelli, M.,Murachelli, A.G.,Confalonieri, S.,Magri, L.,Musacchio, A.,Di Fiore, P.P.,Polo, S.,Schneider, T.R. Crystal Structure of the Ubiquitin Binding Domains of Rabex-5 Reveals Two Modes of Interaction with Ubiquitin. Cell(Cambridge,Mass.), 124:1183-, 2006 Cited by PubMed Abstract: The interaction between ubiquitinated proteins and intracellular proteins harboring ubiquitin binding domains (UBDs) is critical to a multitude of cellular processes. Here, we report that Rabex-5, a guanine nucleotide exchange factor for Rab5, binds to Ub through two independent UBDs. These UBDs determine a number of properties of Rabex-5, including its coupled monoubiquitination and interaction in vivo with ubiquitinated EGFRs. Structural and biochemical characterization of the UBDs of Rabex-5 revealed that one of them (MIU, motif interacting with ubiquitin) binds to Ub with modes superimposable to those of the UIM (ubiquitin-interacting motif):Ub interaction, although in the opposite orientation. The other UBD, RUZ (Rabex-5 ubiquitin binding zinc finger) binds to a surface of Ub centered on Asp58(Ub) and distinct from the "canonical" Ile44(Ub)-based surface. The two binding surfaces allow Ub to interact simultaneously with different UBDs, thus opening new perspectives in Ub-mediated signaling. PubMed: 16499958DOI: 10.1016/J.CELL.2006.02.020 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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