From Proteopedia
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| 1lqb, resolution 2.00Å ()
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| Ligands:
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| Non-Standard Residues:
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| Structural annotation:
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| 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
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| Resources:
| FirstGlance, OCA, RCSB, PDBsum
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| Coordinates:
| save as pdb, mmCIF, xml
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Crystal structure of a hydroxylated HIF-1 alpha peptide bound to the pVHL/elongin-C/elongin-B complex
Template:ABSTRACT PUBMED 12050673
About this Structure
1LQB is a 4 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Hon WC, Wilson MI, Harlos K, Claridge TD, Schofield CJ, Pugh CW, Maxwell PH, Ratcliffe PJ, Stuart DI, Jones EY. Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL. Nature. 2002 Jun 27;417(6892):975-8. Epub 2002 Jun 5. PMID:12050673 doi:http://dx.doi.org/10.1038/nature00767
Page seeded by OCA on Tue Feb 17 21:17:59 2009
Categories: Homo sapiens | Claridge, T D. | Harlos, K. | Hon, W C. | Jones, E Y. | Maxwell, P H. | Pugh, C W. | Ratcliffe, P J. | Schofield, C J. | Stuart, D I. | Wilson, M I. | Cancer | Prolyl hydroxylation | Protein-peptide complex | Proteosomal degradation | Tumor suppressor | Ubiquitin