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Nearest-neighbour analysis of myoglobin antigenic sites. Nearest-neighbour residues whose replacement can alter the environment of binding-site residue(s) and thus change their characteristics and binding capability.

机译：肌红蛋白抗原位点的最近邻分析。最近邻的残基其替代可以改变结合位点残基的环境从而改变其特征和结合能力。

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摘要

By using the known antigenic structure of sperm-whale myoglobin previously determined in this laboratory and the X-ray co-ordinates for the myoglobin molecule, we have calculated the nearest-atom distances between each of the residues of the antigenic sites and all the other amino acids of the myoglobin molecule. These calculations have enabled us to identify the nearest-neighbour residues to each of the residues in the five antigenic sites, and which thus describe the immediate molecular environment of the sites. The influences of chemical changes or replacements in these environmental residues on the binding capacity of an antigenic site, when considered together with replacements directly in the antigenic sites, are expected to account for the major effects and will be extremely useful in explaining the cross-reactions of myoglobins from various species. However, it is stressed that the analysis has limitations due to the qualitative estimates of the effects, the influences of substitutions of once-removed or even at more distant locations (especially when they are cumulative) and finally the influences of any conformational re-adjustments when these occur as a result of the replacement(s).

机译：通过使用先前在本实验室中确定的精鲸鲸鱼肌红蛋白的已知抗原结构以及肌红蛋白分子的X射线坐标，我们计算了抗原位点的每个残基与所有其他残基之间的最近原子距离肌红蛋白分子的氨基酸。这些计算使我们能够鉴定出五个抗原性位点中与每个残基最接近的残基，从而描述了该位点的直接分子环境。与直接在抗原性位点中的置换一起考虑时，这些环境残基中的化学变化或置换对抗原性位点的结合能力的影响预计将起到主要作用，并且在解释交叉反应时将非常有用来自各种物种的肌球蛋白。但是，需要强调的是，由于效果的定性估计，曾经被移除甚至在更远的位置（尤其是当它们累积时）的替换的影响，以及最终任何构象重新调整的影响，该分析都存在局限性当这些由于更换而发生时。

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期刊名称 Biochemical Journal
作者
A L Kazim; M Z Atassi;
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作者单位

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年(卷),期 1980(191),3
年度 1980
页码 673–680
总页数 8
原文格式 PDF
正文语种
中图分类分子生物学;
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1. INTERACTIONS AMONG RESIDUES CD3, E7, E10, AND ELL IN MYOGLOBINS - ATTEMPTS TO SIMULATE THE LIGAND-BINDING PROPERTIES OF APLYSIA MYOGLOBIN [J] . Smerdon SJ., Brzozowski AM., Davies GJ., Biochemistry . 1995,第27期

机译：肌珠蛋白中残基CD3，E7，E10和ELL之间的相互作用-试图模拟海参肌红蛋白的配体结合特性
2. INTERACTIONS AMONG RESIDUES CD3, E7, E10, AND ELL IN MYOGLOBINS - ATTEMPTS TO SIMULATE THE LIGAND-BINDING PROPERTIES OF APLYSIA MYOGLOBIN [J] . Smerdon SJ., Brzozowski AM., Davies GJ., Biochemistry . 1995,第27期

机译：肌珠蛋白中残基CD3，E7，E10和ELL之间的相互作用-试图模拟海参肌红蛋白的配体结合特性
3. A method for predicting individual residue contributions to enzyme specificity and binding-site energies, and its application to MTH1 [J] . Stewart James J. P. Journal of molecular modeling . 2016,第11期

机译：预测单个残基对酶特异性和结合位点能量的贡献的方法及其在MTH1中的应用
4. CHEMICAL BINDING OF RADIONUCLIDES IN ASH RESIDUE IN INCINERATION OF WET SPENT ION-EXCHANGE RESINS IN COMPOSITION WITH POWDER METAL FUEL [C] . Michael I. Ojovan, George A. Petrov, Serge A. Dmitriev, International Conference on Radioactive Waste Management and Environmental Remediation . 1999

机译：粉剂金属燃料中湿法离子交换树脂焚烧灰渣中的化学结合
5. Changing 14 Residues in the Active Site of NPr can Change its Function to that of HPr and P-type ATPase Analysis in Archaea, Spirochetes and Across All Known Domains of Life [D] . Chan, Henry. 2010

机译：在古细菌，螺旋体和所有已知生命域中，改变NPr活性位点中的14个残基可以将其功能更改为HPr和P型ATPase分析。
6. Distance calculation of residues neighbouring to lysozyme antigenic sites. Site-neighbouring residues whose evolutionary substitution can modify the characteristics and binding energy of the sites. [O] . M Z Atassi, A L Kazim 1980

机译：溶菌酶抗原位点附近残基的距离计算。进化取代可以改变位点的特征和结合能的位点相邻残基。
7. Nearest-neighbour analysis of myoglobin antigenic sites. Nearest-neighbour residues whose replacement can alter the environment of binding-site residue(s) and thus change their characteristics and binding capability. [O] . Kazim, A L, Atassi, M Z 1980

机译：肌红蛋白抗原位点的最近邻分析。最近邻的残基，其替代可以改变结合位点残基的环境，从而改变其特征和结合能力。

Nearest-neighbour analysis of myoglobin antigenic sites. Nearest-neighbour residues whose replacement can alter the environment of binding-site residue(s) and thus change their characteristics and binding capability.

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