I I Mathews,A Tulinsky
I I Mathews
The structures of two mimetic inhibitor complexes of human alpha-thrombin have been determined by X-ray crystallography. One mimics a beta-turn with a bicyclic ring system; the other mimics two different active-site binding modes. The beta-...
Molecular dynamics and structure-based drug design for predicting non-natural nonapeptide binding to a class I MHC protein [0.03%]
基于分子动力学和结构的药物设计预测非天然九肽与I类MHCI类蛋白结合力的研究
L Scapozza,D Rognan,G Folkers et al.
L Scapozza et al.
Starting from the known three-dimensional structure of the class I major histocompatibility complex-encoded HLA-B*2705 protein, three non-natural nonapeptides were designed to fit optimally the HLA-B*2705-binding groove. The optimization wa...
Calculation of relative binding affinities of purine nucleoside phosphorylase inhibitors [0.03%]
嘌呤核糖磷酸化酶抑制剂结合亲和力的计算
M Carson,Z Yang,Y S Babu et al.
M Carson et al.
The competitive binding of inhibitors to purine nucleoside phosphorylase (PNP) has been experimentally measured. Fast and reliable computational methods to estimate binding would allow assessment of any proposed inhibitor before its synthes...
Y S Babu,S E Ealick,C E Bugg et al.
Y S Babu et al.
Inhibitors of purine nucleoside phosphorylase may have therapeutic value in the treatment of T-cell proliferative diseases such as T-cell leukemia, in the suppression of host-versus-graft response in organ transplants, and in the treatment ...
Design, synthesis and structure of non-macrocyclic inhibitors of FKBP12, the major binding protein for the immunosuppressant FK506 [0.03%]
非免疫抑制剂FK506主要结合蛋白FKBP12的非大环抑制剂的设计、合成和结构研究
D M Armistead,M C Badia,D D Deininger et al.
D M Armistead et al.
We have synthesized a series of non-macrocyclic ligands to FKBP12 that are comparable in binding potency and peptidyl prolyl isomerase (PPIase) inhibition to FK506 itself. We have also solved the structure of one of these ligands in complex...
Comparative X-ray structures of the major binding protein for the immunosuppressant FK506 (tacrolimus) in unliganded form and in complex with FK506 and rapamycin [0.03%]
FK506(他克莫司)和雷帕霉素复合物与未结合形式的主要免疫抑制剂受体蛋白的比较X-射线结构分析
K P Wilson,M M Yamashita,M D Sintchak et al.
K P Wilson et al.
FK506 (tacrolimus) is a natural product now approved in the US and Japan for organ transplantation. FK506, in complex with its 12 kDa cytosolic receptor (FKBP12), is a potent agonist of immunosuppression through the inhibition of the phosph...
M Luo,M J Jedrzejas,S Singh et al.
M Luo et al.
A strategy was developed to design non-carbohydrate inhibitors of influenza virus neuraminidase. Using an iterative cycle of modeling, synthesis, biological testing and X-ray crystallography structure determination, a series of inhibitors b...
Structures of four methyltetrazole-containing antiviral compounds in human rhinovirus serotype 14 [0.03%]
四种含甲基四氮唑抗病毒化合物的人类鼻病毒14型晶体结构
V L Giranda,G R Russo,P J Felock et al.
V L Giranda et al.
Four novel antiviral WIN compounds, that contain a methyl tetrazole ring as well as isoxazole, pyridazine or acetylfuran rings, have had their structures determined in human rhinovirus serotype 14 at 2.9 A resolution. These compounds bind i...
WIN51711-resistant mutants of poliovirus type 3: capsid residues important in uncoating functions [0.03%]
脊髓灰质炎病毒3型WIN51711耐药突变体的研究：衣壳上在脱壳功能中起重要作用的残基
A G Mosser,J Y Sgro,R R Rueckert
A G Mosser
Capsid-binding drugs that inhibit the first stage of picornaviral uncoating were used to select drug-resistant mutants of the Sabin strain of poliovirus type 3. Such mutants provide information about parts of the capsid that are important f...
Binding of the antiviral drug WIN51711 to the sabin strain of type 3 poliovirus: structural comparison with drug binding in rhinovirus 14 [0.03%]
抗病毒药物WIN51711与脊髓灰质炎病毒萨宾III型结合：与WIN51711在鼻病毒14中结合的结构比较
C N Hiremath,R A Grant,D J Filman et al.
C N Hiremath et al.
The crystal structure of the Sabin strain of type 3 poliovirus (P3/Sabin) complexed with the antiviral drug WIN51711 has been determined at 2.9 A resolution. Drugs of this kind are known to inhibit the uncoating of the virus during infectio...