Sandbox UC 14

'HOLA!!' hola jaja

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3nnq, resolution 2.69Å ()

Ligands:

,

Non-Standard Residues:

Gene:

gag-pol (Moloney murine leukemia virus)

Structural annotation:
Resources:	InterPro : Ipr000477, Ipr002156, Ipr021109, Ipr018061, Ipr013084, Ipr012337, Ipr010999, Ipr009007, Ipr003036, Ipr002079, Ipr001995, Ipr001969, Ipr001878, Ipr001584, Ipr000840

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

N-terminal domain of Moloney murine leukemia virus integraseN-terminal domain of Moloney murine leukemia virus integrase

Publication Abstract from PubMed

The essential mammalian enzyme O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, here OGT) couples metabolic status to the regulation of a wide variety of cellular signalling pathways by acting as a nutrient sensor. OGT catalyses the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine (UDP-GlcNAc) to serines and threonines of cytoplasmic, nuclear and mitochondrial proteins, including numerous transcription factors, tumour suppressors, kinases, phosphatases and histone-modifying proteins. Aberrant glycosylation by OGT has been linked to insulin resistance, diabetic complications, cancer and neurodegenerative diseases including Alzheimer's. Despite the importance of OGT, the details of how it recognizes and glycosylates its protein substrates are largely unknown. We report here two crystal structures of human OGT, as a binary complex with UDP (2.8 A resolution) and as a ternary complex with UDP and a peptide substrate (1.95 A). The structures provide clues to the enzyme mechanism, show how OGT recognizes target peptide sequences, and reveal the fold of the unique domain between the two halves of the catalytic region. This information will accelerate the rational design of biological experiments to investigate OGT's functions; it will also help the design of inhibitors for use as cellular probes and help to assess its potential as a therapeutic target.

Structure of human O-GlcNAc transferase and its complex with a peptide substrate., Lazarus MB, Nam Y, Jiang J, Sliz P, Walker S, Nature. 2011 Jan 27;469(7331):564-7. Epub 2011 Jan 16. PMID:21240259

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Cuadro azulCuadro azul

hola ^[1] como estas ^[2]

Escena colorea la proteina desde en N terminal al C terminal.

Acetilcolinesterase

Escenade otra proteina en su interaccion con , esto es de practica.

Structure of N-terminal domain of Moloney murine leukemia virus integrase (PDB entry 3nnq)

Drag the structure with the mouse to rotate

ReferenciasReferencias

↑ Lecompte F, Sinet M, Azoulay E, Muffat-Joly M, Pocidalo JJ. Oxygen transport by haemoglobin. A comparison of whole blood, washed erythrocytes and haemoglobin solution. Biomedicine. 1975 Jun 30;23(6):226-9. PMID:2345
↑ Nair BM, Oste R, Asp NG, Dahlqvist A. Enzymatic hydrolysis of food protein for amino acid analysis. I. Solubilization of the protein. J Agric Food Chem. 1976 Mar-Apr;24(2):386-9. PMID:3533

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[1] Lecompte F, Sinet M, Azoulay E, Muffat-Joly M, Pocidalo JJ. Oxygen transport by haemoglobin. A comparison of whole blood, washed erythrocytes and haemoglobin solution. Biomedicine. 1975 Jun 30;23(6):226-9. PMID:2345

[2] Nair BM, Oste R, Asp NG, Dahlqvist A. Enzymatic hydrolysis of food protein for amino acid analysis. I. Solubilization of the protein. J Agric Food Chem. 1976 Mar-Apr;24(2):386-9. PMID:3533

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