1lqb

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spinqualitylabelsall models PDB ID 1lqb Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1lqb, resolution 2.00Å ()
Ligands:
Non-Standard Residues:
Structural annotation: Resources: CATH : 1Lqba00, 1Lqbb00, 1Lqbc01, 1Lqbc02 InterPro : Ipr000626, Ipr001232, Ipr011333, Ipr002714, Ipr011598, Ipr013655, Ipr000014, Ipr000700, Ipr001610, Ipr001321, Ipr014887, Ipr001092 Pfam : PF03931, PF01847 SCOP : d1lqba_, d1lqbb_, d1lqbc_ UniProt : Q15370, Q15369, P40337, Q16665
Functional annotation: Cellular component: nucleus cytoplasm membrane cytosol mitochondrion endoplasmic reticulum Biological process: protein complex assembly regulation of transcription, DNA-dependent transcription ubiquitin cycle RNA elongation from RNA polymerase II promoter protein modification process regulation of transcription from RNA polymerase II promoter cell cycle anti-apoptosis negative regulation of cell proliferation positive regulation of cell differentiation protein ubiquitination negative regulation of transcription from RNA polymerase II promoter cell morphogenesis response to stress negative regulation of cell cycle proteolysis protein stabilization homeostatic process signal transduction response to hypoxia transcription, DNA-dependent positive regulation of transcription regulation of transcription Molecular function: protein binding transcription elongation regulator activity transcription factor binding signal transducer activity transcription regulator activity histone acetyltransferase binding DNA binding RNA polymerase II transcription factor activity, enhancer binding transcription factor activity protein heterodimerization activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Crystal structure of a hydroxylated HIF-1 alpha peptide bound to the pVHL/elongin-C/elongin-B complex

Overview

Hypoxia-inducible factor-1 (HIF-1) is a transcriptional complex that controls cellular and systemic homeostatic responses to oxygen availability. HIF-1 alpha is the oxygen-regulated subunit of HIF-1, an alpha beta heterodimeric complex. HIF-1 alpha is stable in hypoxia, but in the presence of oxygen it is targeted for proteasomal degradation by the ubiquitination complex pVHL, the protein of the von Hippel Lindau (VHL) tumour suppressor gene and a component of an E3 ubiquitin ligase complex. Capture of HIF-1 alpha by pVHL is regulated by hydroxylation of specific prolyl residues in two functionally independent regions of HIF-1 alpha. The crystal structure of a hydroxylated HIF-1 alpha peptide bound to VCB (pVHL, elongins C and B) and solution binding assays reveal a single, conserved hydroxyproline-binding pocket in pVHL. Optimized hydrogen bonding to the buried hydroxyprolyl group confers precise discrimination between hydroxylated and unmodified prolyl residues. This mechanism provides a new focus for development of therapeutic agents to modulate cellular responses to hypoxia.

About this Structure

1LQB is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL., Hon WC, Wilson MI, Harlos K, Claridge TD, Schofield CJ, Pugh CW, Maxwell PH, Ratcliffe PJ, Stuart DI, Jones EY, Nature. 2002 Jun 27;417(6892):975-8. Epub 2002 Jun 5. PMID:12050673 Page seeded by OCA on Sat May 3 00:10:19 2008