2vh5

CRYSTAL STRUCTURE OF HRAS(G12V) - ANTI-RAS FV (DISULFIDE FREE MUTANT) COMPLEX

spinqualitylabelsall models 2vh5, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vh5 is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GTP, MG, ZN Related: 121p, 1aa9, 1agp, 1bkd, 1crr, 1ctq, 1gnr, 1iaq, 1jai, 1lf0, 1nvu, 1nvv, 1nvw, 1nvx, 1p2s, 1plk, 1qra, 1rvd, 1wq1, 1xcm, 1xd2, 1zvq, 1zw6, 2c5l, 2cl6, 2cl7, 2clc, 2cld, 1clu, 1crp, 1crq, 1gnp, 1gnq, 1he8, 1ioz, 1jah, 1k8r, 1lf5, 1lfd, 1p2t, 1p2u, 1p2v, 1pll, 1q21, 1xj0, 221p, 2ce2, 2cl0, 2gdp, 2q21, 2uzi, 4q21, 5p21, 621p, 6q21, 821p, 2evw, 421p, 521p, 721p Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [RASH_HUMAN] Defects in HRAS are the cause of faciocutaneoskeletal syndrome (FCSS) [MIM:218040]. A rare condition characterized by prenatally increased growth, postnatal growth deficiency, mental retardation, distinctive facial appearance, cardiovascular abnormalities (typically pulmonic stenosis, hypertrophic cardiomyopathy and/or atrial tachycardia), tumor predisposition, skin and musculoskeletal abnormalities. Defects in HRAS are the cause of congenital myopathy with excess of muscle spindles (CMEMS) [MIM:218040]. CMEMS is a variant of Costello syndrome. Defects in HRAS may be a cause of susceptibility to Hurthle cell thyroid carcinoma (HCTC) [MIM:607464]. Hurthle cell thyroid carcinoma accounts for approximately 3% of all thyroid cancers. Although they are classified as variants of follicular neoplasms, they are more often multifocal and somewhat more aggressive and are less likely to take up iodine than are other follicular neoplasms. Note=Mutations which change positions 12, 13 or 61 activate the potential of HRAS to transform cultured cells and are implicated in a variety of human tumors. Defects in HRAS are a cause of susceptibility to bladder cancer (BLC) [MIM:109800]. A malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. Most bladder cancers are transitional cell carcinomas. They begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences. Note=Defects in HRAS are the cause of oral squamous cell carcinoma (OSCC). Defects in HRAS are the cause of Schimmelpenning-Feuerstein-Mims syndrome (SFM) [MIM:163200]. A disease characterized by sebaceous nevi, often on the face, associated with variable ipsilateral abnormalities of the central nervous system, ocular anomalies, and skeletal defects. Many oral manifestations have been reported, not only including hypoplastic and malformed teeth, and mucosal papillomatosis, but also ankyloglossia, hemihyperplastic tongue, intraoral nevus, giant cell granuloma, ameloblastoma, bone cysts, follicular cysts, oligodontia, and odontodysplasia. Sebaceous nevi follow the lines of Blaschko and these can continue as linear intraoral lesions, as in mucosal papillomatosis. Function [RASH_HUMAN] Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Functional intracellular antibody fragments do not require invariant intra-domain disulfide bonds.,Tanaka T, Rabbitts TH J Mol Biol. 2008 Feb 22;376(3):749-57. Epub 2007 Dec 4. PMID:18187153 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also GTPase HRas

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