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Beta gamma-crystallin redux. -晶体蛋白还原。
Nature Structural Biology
Pub Date : 1996-08-01
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引用次数: 0
'Diamond' under the hammer? 锤子下的“钻石”?
Nature Structural Biology
Pub Date : 1995-12-01
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引用次数: 0
Battle for BMRB Biological Magnetic Resonance Data Bank. BMRB生物磁共振数据库之战。
Nature Structural Biology
Pub Date : 1995-10-01
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引用次数: 0
Picture story. Pax and paired. 图片故事。和平共处，成双成对。
Nature Structural Biology
Pub Date : 1995-04-01
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引用次数: 0
Picture story. Interacting with actin. 图片故事。与肌动蛋白相互作用。
Nature Structural Biology
Pub Date : 1995-04-01
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引用次数: 0
Picture story. Bluetongue's sticky bristle. 图片故事。蓝舌病的粘毛。
Nature Structural Biology
Pub Date : 1995-02-01
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引用次数: 0
Residues defining V beta specificity in staphylococcal enterotoxins. 葡萄球菌肠毒素中定义V β特异性的残基。
Nature Structural Biology
Pub Date : 1995-01-01 DOI: 10.2210/pdb1sea/pdb
S. Swaminathan, W. Furey, J. Pletcher, M. Sax
The three-dimensional structure of staphylococcal enterotoxin C2 has been determined at 2.7 A resolution by x-ray diffraction, while the structures of enterotoxins A and E have been modelled based on their sequence homology to other staphylococcal enterotoxins. The T-cell receptor-binding sites of staphylococcal enterotoxin (SE) B and SEC2 are compared and the stereochemical interactions likely to be responsible for their differing V beta specificities are identified. A similar comparison is made between SEA and SEE.
通过x射线衍射在2.7 A分辨率下确定了葡萄球菌肠毒素C2的三维结构，而肠毒素A和E的结构基于它们与其他葡萄球菌肠毒素的序列同源性建立了模型。比较了葡萄球菌肠毒素(SE) B和SEC2的t细胞受体结合位点，并确定了可能导致其不同V β特异性的立体化学相互作用。SEA和SEE之间也进行了类似的比较。
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引用次数: 20
Picture story. Heads you bind, tails you bind.SH3 domains. 图片故事。正面归正面，反面归反面。SH3区域。
Nature Structural Biology
Pub Date : 1995-01-01
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引用次数: 0
Picture story. Birds of a feather. 图片故事。物以类聚。
Nature Structural Biology
Pub Date : 1994-12-01
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引用次数: 0
Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor. 果蝇热休克转录因子dna结合域的溶液结构。
Nature Structural Biology
Pub Date : 1994-09-01
G W Vuister, S J Kim, A Orosz, J Marquardt, C Wu, A Bax

The solution structure of the DNA-binding domain of the Drosophila heat shock transcription factor, as determined by multidimensional multinuclear NMR, resembles that of the helix-turn-helix class of DNA-binding proteins. The domain comprises a four-stranded antiparallel beta-sheet, packed against a three-helix bundle. The second helix is significantly distorted and is separated from the third helix by an extended turn which is subject to conformational averaging on an intermediate time scale. Helix 3 forms a classical amphipathic helix with polar and charged residues exposed to the solvent. Upon titration with DNA, resonance shifts in the backbone and Asn and Gln side-chain amides indicate that helix 3 acts as the recognition helix of the heat shock transcription factor.

果蝇热休克转录因子的dna结合域的溶液结构，由多维多核核磁共振确定，类似于螺旋-螺旋-螺旋类dna结合蛋白。该结构域包括一个反平行的四股β -片，围绕着一个三螺旋束。第二螺旋明显扭曲，并与第三螺旋通过一个延长的转弯分离，这是在中间时间尺度上的构象平均。螺旋3与暴露在溶剂中的极性和带电残基形成经典的两亲螺旋。用DNA滴定后，主链和Asn和Gln侧链酰胺的共振位移表明螺旋3是热休克转录因子的识别螺旋。
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引用次数: 0
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