| pubmed-article:18833280 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18833280 | lifeskim:mentions | umls-concept:C0441471 | lld:lifeskim |
| pubmed-article:18833280 | lifeskim:mentions | umls-concept:C0205374 | lld:lifeskim |
| pubmed-article:18833280 | lifeskim:mentions | umls-concept:C0917721 | lld:lifeskim |
| pubmed-article:18833280 | pubmed:issue | 7213 | lld:pubmed |
| pubmed-article:18833280 | pubmed:dateCreated | 2008-10-3 | lld:pubmed |
| pubmed-article:18833280 | pubmed:abstractText | HIV-1 protease processes the Gag and Gag-Pol polyproteins into mature structural and functional proteins, including itself, and is therefore indispensable for viral maturation. The mature protease is active only as a dimer with each subunit contributing catalytic residues. The full-length transframe region protease precursor appears to be monomeric yet undergoes maturation via intramolecular cleavage of a putative precursor dimer, concomitant with the appearance of mature-like catalytic activity. How such intramolecular cleavage can occur when the amino and carboxy termini of the mature protease are part of an intersubunit beta-sheet located distal from the active site is unclear. Here we visualize the early events in N-terminal autoprocessing using an inactive mini-precursor with a four-residue N-terminal extension that mimics the transframe region protease precursor. Using paramagnetic relaxation enhancement, a technique that is exquisitely sensitive to the presence of minor species, we show that the mini-precursor forms highly transient, lowly populated (3-5%) dimeric encounter complexes that involve the mature dimer interface but occupy a wide range of subunit orientations relative to the mature dimer. Furthermore, the occupancy of the mature dimer configuration constitutes a very small fraction of the self-associated species (accounting for the very low enzymatic activity of the protease precursor), and the N-terminal extension makes transient intra- and intersubunit contacts with the substrate binding site and is therefore available for autocleavage when the correct dimer orientation is sampled within the encounter complex ensemble. | lld:pubmed |
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| pubmed-article:18833280 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18833280 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18833280 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18833280 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18833280 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18833280 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:18833280 | pubmed:issn | 1476-4687 | lld:pubmed |
| pubmed-article:18833280 | pubmed:author | pubmed-author:TangChunC | lld:pubmed |
| pubmed-article:18833280 | pubmed:author | pubmed-author:LouisJohn MJM | lld:pubmed |
| pubmed-article:18833280 | pubmed:author | pubmed-author:CloreG... | lld:pubmed |
| pubmed-article:18833280 | pubmed:author | pubmed-author:SuhJeong-Yong... | lld:pubmed |
| pubmed-article:18833280 | pubmed:author | pubmed-author:AnianaAnnieA | lld:pubmed |
| pubmed-article:18833280 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18833280 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:18833280 | pubmed:volume | 455 | lld:pubmed |
| pubmed-article:18833280 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18833280 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18833280 | pubmed:pagination | 693-6 | lld:pubmed |
| pubmed-article:18833280 | pubmed:dateRevised | 2010-9-21 | lld:pubmed |
| pubmed-article:18833280 | pubmed:meshHeading | pubmed-meshheading:18833280... | lld:pubmed |
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| pubmed-article:18833280 | pubmed:meshHeading | pubmed-meshheading:18833280... | lld:pubmed |
| pubmed-article:18833280 | pubmed:meshHeading | pubmed-meshheading:18833280... | lld:pubmed |
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| pubmed-article:18833280 | pubmed:meshHeading | pubmed-meshheading:18833280... | lld:pubmed |
| pubmed-article:18833280 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18833280 | pubmed:articleTitle | Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease. | lld:pubmed |
| pubmed-article:18833280 | pubmed:affiliation | Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA. | lld:pubmed |
| pubmed-article:18833280 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18833280 | pubmed:publicationType | Research Support, N.I.H., Intramural | lld:pubmed |
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