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首页> 外文期刊>Journal of Molecular Biology >THE AMINO-TERMINAL RESIDUES IN THE CRYSTAL STRUCTURE OF CONNECTIVE TISSUE ACTIVATING PEPTIDE-III (DES10) BLOCK THE ELR CHEMOTACTIC SEQUENCE
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THE AMINO-TERMINAL RESIDUES IN THE CRYSTAL STRUCTURE OF CONNECTIVE TISSUE ACTIVATING PEPTIDE-III (DES10) BLOCK THE ELR CHEMOTACTIC SEQUENCE

机译：结缔组织活化肽-III（DES10）晶体结构中的氨基末端残基阻碍了Elr的化学序列

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alpha-Chemokines comprise a family of cytokines that are chemotactic for neutrophils and have a structure similar to platelet factor 4 (PF4), in which the first two cysteine residues are separated by one residue (Cys-X-Cys). The two alpha-chemokines, connective tissue activating peptide-III (CTAP-III) and neutrophil activating peptide-2 (NAP-2), are carboxyl-terminal fragments of platelet basic protein (PBP) that are generated by monocyte-derived proteases. NAP-2 strongly stimulates neutrophils that are present during inflammation whereas its precursors, PBP and CTAP-III, are inactive, although they also possess the highly conserved, aminoterminal sequence, Glu-Leu-Arg (ELR), that is critical for receptor binding. To resolve this conundrum, we have determined the crystal structure of recombinant Asp-CTAP, which has ten fewer amino-terminal residues than CTAP-III but five more than NAP-2. The space group is P2(1), with unit cell dimensions a = 43.8 Angstrom, b = 76.8 Angstrom, c = 43.8 Angstrom, and beta = 97.0 degrees, and a tetramer in the asymmetric unit. The molecular replacement method, with the NAP-2 tetramer as a starting model, was used to determine the initial phase information. The final R-factor is 0.196 (R(free) = 0.251) for 2 sigma data from 7.0 to 1.75 Angstrom resolution. This high-resolution model of Asp-CTAP is the longest defined structure of an alpha-chemokine to date. The electron density map shows an over-all structure for Asp-CTAP that is very similar to that of NAP-2, but with the additional five amino-terminal residues folding back through a type-II turn, thereby stabilizing the oligomeric ''inactive'' state, and masking the critical ELR receptor binding region that is exposed in the structure of NAP-2. (C) 1997 Academic Press Limited. [References: 76]
机译：α-趋化因子包含对嗜中性粒细胞具有趋化性的细胞因子家族，其结构类似于血小板因子4（PF4），其中前两个半胱氨酸残基被一个残基（Cys-X-Cys）隔开。结缔组织激活肽III（CTAP-III）和嗜中性粒细胞激活肽2（NAP-2）这两个α趋化因子是单核细胞衍生的蛋白酶产生的血小板碱性蛋白（PBP）的羧基末端片段。 NAP-2强烈刺激炎症过程中存在的嗜中性粒细胞，而其前体PBP和CTAP-III没有活性，尽管它们也具有高度保守的氨基末端序列Glu-Leu-Arg（ELR），这对于受体结合至关重要。为了解决这个难题，我们确定了重组Asp-CTAP的晶体结构，该结构的氨基末端残基比CTAP-III少十个，但比NAP-2多五个。该空间群为P2（1），单位晶胞尺寸为a = 43.8埃，b = 76.8埃，c = 43.8埃，β= 97.0度，四聚体位于不对称单元中。以NAP-2四聚体为起始模型的分子置换方法用于确定初始相信息。对于7.0至1.75埃分辨率的2 sigma数据，最终的R因子为0.196（R（自由）= 0.251）。 Asp-CTAP的高分辨率模型是迄今为止定义的最长的α-趋化因子结构。电子密度图显示了与NAP-2非常相似的Asp-CTAP的总体结构，但另外五个氨基末端残基通过II型转折折叠回来，从而稳定了低聚的``无活性''状态，并掩盖在NAP-2结构中暴露的关键ELR受体结合区。 （C）1997 Academic Press Limited。 [参考：76]

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