2VH5
CRYSTAL STRUCTURE OF HRAS(G12V) - ANTI-RAS FV (disulfide free mutant) COMPLEX
Summary for 2VH5
| Entry DOI | 10.2210/pdb2vh5/pdb |
| Related | 121P 1AA9 1AGP 1BKD 1CLU 1CRP 1CRQ 1CRR 1CTQ 1GNP 1GNQ 1GNR 1HE8 1IAQ 1IOZ 1JAH 1JAI 1K8R 1LF0 1LF5 1LFD 1NVU 1NVV 1NVW 1NVX 1P2S 1P2T 1P2U 1P2V 1PLK 1PLL 1Q21 1QRA 1RVD 1WQ1 1XCM 1XD2 1XJ0 1ZVQ 1ZW6 221P 2C5L 2CE2 2CL0 2CL6 2CL7 2CLC 2CLD 2EVW 2GDP 2Q21 2UZI 421P 4Q21 521P 5P21 621P 6Q21 721P 821P |
| Descriptor | ANTI-RAS FV HEAVY CHAIN, ANTI-RAS FV LIGHT CHAIN, GTPASE HRAS, ... (7 entities in total) |
| Functional Keywords | immunoglobulin domain, signaling protein/immune system, methylation, prenylation, lipoprotein, gtp-binding, signal transduction, nucleotide- binding, disease mutation, nucleotide-binding, immune system, membrane, oncogene, antibody, palmitate, intrabody, proto-oncogene, cancer therapy, golgi apparatus |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Cellular location | Cell membrane. Isoform 2: Nucleus: P01112 |
| Total number of polymer chains | 3 |
| Total formula weight | 43497.57 |
| Authors | Tanaka, T.,Williams, R.L.,Rabbitts, T.H. (deposition date: 2007-11-19, release date: 2008-01-22, Last modification date: 2024-05-08) |
| Primary citation | Tanaka, T.,Rabbitts, T.H. Functional Intracellular Antibody Fragments Do not Require Invariant Intra-Domain Disulfide Bonds. J.Mol.Biol., 376:749-, 2008 Cited by PubMed Abstract: Intracellular antibody fragments that interfere with molecular interactions inside cells are valuable in investigation of interactomes and in therapeutics, but their application demands that they function in the reducing cellular milieu. We show here a 2.7-A crystal structure of intracellular antibody folds based on scaffolds developed from intracellular antibody capture technology, and we reveal that there is no structural or functional difference with or without the intra-domain disulfide bond of the variable domain of heavy chain or the variable domain of light chain. The data indicate that, in the reducing in vivo environment, the absence of the intra-domain disulfide bond is not an impediment to correction of antibody folding or to interaction with antigen. Thus, the structural constraints for in-cell function are intrinsic to variable single-domain framework sequences, providing a generic scaffold for isolation of functional intracellular antibody single domains. PubMed: 18187153DOI: 10.1016/J.JMB.2007.11.085 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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