pubmed-article:19273847 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19273847 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
pubmed-article:19273847 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:19273847 | lifeskim:mentions | umls-concept:C0043309 | lld:lifeskim |
pubmed-article:19273847 | lifeskim:mentions | umls-concept:C0010424 | lld:lifeskim |
pubmed-article:19273847 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:19273847 | lifeskim:mentions | umls-concept:C0027946 | lld:lifeskim |
pubmed-article:19273847 | lifeskim:mentions | umls-concept:C0174543 | lld:lifeskim |
pubmed-article:19273847 | lifeskim:mentions | umls-concept:C0917721 | lld:lifeskim |
pubmed-article:19273847 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:19273847 | pubmed:dateCreated | 2009-3-25 | lld:pubmed |
pubmed-article:19273847 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19273847 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19273847 | pubmed:abstractText | HIV-1 protease is a dimeric aspartic protease that plays an essential role in viral replication. To further understand the catalytic mechanism and inhibitor recognition of HIV-1 protease, we need to determine the locations of key hydrogen atoms in the catalytic aspartates Asp-25 and Asp-125. The structure of HIV-1 protease in complex with transition-state analog KNI-272 was determined by combined neutron crystallography at 1.9-A resolution and X-ray crystallography at 1.4-A resolution. The resulting structural data show that the catalytic residue Asp-25 is protonated and that Asp-125 (the catalytic residue from the corresponding diad-related molecule) is deprotonated. The proton on Asp-25 makes a hydrogen bond with the carbonyl group of the allophenylnorstatine (Apns) group in KNI-272. The deprotonated Asp-125 bonds to the hydroxyl proton of Apns. The results provide direct experimental evidence for proposed aspects of the catalytic mechanism of HIV-1 protease and can therefore contribute substantially to the development of specific inhibitors for therapeutic application. | lld:pubmed |
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pubmed-article:19273847 | pubmed:language | eng | lld:pubmed |
pubmed-article:19273847 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19273847 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19273847 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19273847 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:19273847 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19273847 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19273847 | pubmed:month | Mar | lld:pubmed |
pubmed-article:19273847 | pubmed:issn | 1091-6490 | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:AraiShigekiS | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:HonjoEijiroE | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:KimuraTooruT | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:KisoYoshiakiY | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:MatsumuraHiro... | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:TakanoKazufum... | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:KurokiRyotaR | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:TamadaTaroT | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:HayashiYoshio... | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:AdachiMotoyas... | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:SugiyamaShige... | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:AdachiHiroaki... | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:MoriYusukeY | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:OhharaTakashi... | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:HidakaKoushiK | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:KuriharaKazuo... | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:OkazakiNobuoN | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:KimuraKanameK | lld:pubmed |
pubmed-article:19273847 | pubmed:author | pubmed-author:ShoyamaYoshin... | lld:pubmed |
pubmed-article:19273847 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19273847 | pubmed:day | 24 | lld:pubmed |
pubmed-article:19273847 | pubmed:volume | 106 | lld:pubmed |
pubmed-article:19273847 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19273847 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19273847 | pubmed:pagination | 4641-6 | lld:pubmed |
pubmed-article:19273847 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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