Structure of the Insect Cytokine Peptide Plasmatocyte-spreading Peptide 1 from Pseudoplusia includens *
Structure of the Insect Cytokine Peptide Plasmatocyte-spreading Peptide 1 from Pseudoplusia includens *
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来自 Pseudoplusia includens 的昆虫细胞因子肽浆细胞传播肽 1 的结构 *
DOI：
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发表时间：
1999
影响因子：
4.8
通讯作者：
J. Markley
中科院分区：
文献类型：
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作者：
B. Volkman;M. Anderson;K. Clark;Y. Hayakawa;M. Strand;J. Markley
最近确定的浆细胞扩展肽从蛾Pseudoplusia includens（PSP 1）的结构已被确定的NMR光谱。这种新型昆虫细胞因子由23个氨基酸残基和一个二硫键组成。利用总共337个距离约束的扭转角动力学计算产生了30个结构的系综，残基7-22的平均骨架均方根偏差与平均结构的偏差为0.18 μ m。该结构由一个无序的N-末端区域和一个明确的核心组成，该核心通过许多疏水相互作用和一个短发夹稳定。结构比较证实，PSP 1采用表皮生长因子（EGF）样折叠与人血栓调节蛋白的EGF样模块5的C-末端亚结构域密切相似。PSP 1的三维结构和EGF-受体相互作用的大量文献相结合，应加速识别负责该免疫调节肽家族的受体结合活性的特定残基的过程。
The structure of the recently identified plasmatocyte spreading peptide from the moth Pseudoplusia includens (PSP1) has been determined by NMR spectroscopy. This novel insect cytokine consists of 23 amino acid residues and a single disulfide bond. Torsion angle dynamics calculations utilizing a total of 337 distance constraints yielded an ensemble of 30 structures with an average backbone root mean square deviation for residues 7–22 of 0.18 Å from the mean structure. The structure consists of a disordered N-terminal region and a well defined core that is stabilized by numerous hydrophobic interactions and a short β-hairpin. Structural comparisons confirm that PSP1 adopts an epidermal growth factor (EGF)-like fold with close similarity to the C-terminal subdomain of EGF-like module 5 of human thrombomodulin. The combination of the three-dimensional structure of PSP1 and the extensive literature on EGF-receptor interactions should accelerate the process of identifying the specific residues responsible for receptor binding activity of this family of immunoregulatory peptides.
与凝血酶复合的血栓调节蛋白第五个 EGF 结构域的九肽结构。
影响因子：
2.9
作者：
Mathews,II;Padmanabhan,KP;Tulinksy,A;Sadler,JE
通讯作者：
Sadler,JE
DOI：
10.1006/bbrc.1998.9145
发表时间：
1998-09-18
影响因子：
3.1
作者：
Clark, KD;Witherell, A;Strand, MR
通讯作者：
Strand, MR