2RRS
NMR Structure of LC4 transmembrane segment of CCR5
Summary for 2RRS
| Entry DOI | 10.2210/pdb2rrs/pdb |
| NMR Information | BMRB: 11439 |
| Descriptor | C-C chemokine receptor type 5 (1 entity in total) |
| Functional Keywords | lc4, ccr5, hiv, transmembrane protein, gpcr, signaling protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane; Multi-pass membrane protein: P51681 |
| Total number of polymer chains | 1 |
| Total formula weight | 1965.30 |
| Authors | Miyamoto, K. (deposition date: 2011-04-11, release date: 2012-04-11, Last modification date: 2024-05-29) |
| Primary citation | Miyamoto, K.,Togiya, K. Solution Structure of LC4 Transmembrane Segment of CCR5 Plos One, 6:e20452-e20452, 2011 Cited by PubMed Abstract: CC-chemokine receptor 5 (CCR5) is a specific co-receptor allowing the entry of human immunodeficiency virus type 1 (HIV-1). The LC4 region in CCR5 is required for HIV-1 entry into the cells. In this study, the solution structure of LC4 in SDS micelles was elucidated by using standard 1H two-dimensional NMR spectroscopy, circular dichroism, and fluorescence quenching. The LC4 structure adopts two helical structures, whereas the C-terminal part remains unstructured. The positions in which LC4 binds to the HIV-1 inhibitory peptide LC5 were determined by docking calculations in addition to NMR data. The poses showed the importance of the hydrophobic interface of the assembled structures. The solution structure of LC4 elucidated in the present work provides a structural basis for further studies on the HIV-1 inhibitory function of the LC4 region. PubMed: 21647380DOI: 10.1371/journal.pone.0020452 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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