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1
Identification of an active site peptide of skeletal myosin after photoaffinity labeling with N-(4-azido-2-nitrophenyl)-2-aminoethyl diphosphate.用N-(4-叠氮基-2-硝基苯基)-2-氨基乙基二磷酸进行光亲和标记后鉴定骨骼肌肌球蛋白的活性位点肽段。
Proc Natl Acad Sci U S A. 1985 Mar;82(6):1575-9. doi: 10.1073/pnas.82.6.1575.
2
Photoaffinity labeling of scallop myosin with 2-[(4-azido-2-nitrophenyl)amino]ethyl diphosphate: identification of an active site arginine analogous to tryptophan-130 in skeletal muscle myosin.用2-[(4-叠氮基-2-硝基苯基)氨基]乙基二磷酸对扇贝肌球蛋白进行光亲和标记：鉴定类似于骨骼肌肌球蛋白中色氨酸-130的活性位点精氨酸。
Bioconjug Chem. 1992 Jul-Aug;3(4):328-36. doi: 10.1021/bc00016a012.
3
2-[(4-Azido-2-nitrophenyl)amino]ethyl triphosphate, a novel chromophoric and photoaffinity analogue of ATP. Synthesis, characterization, and interaction with myosin subfragment 1.2-[(4-叠氮基-2-硝基苯基)氨基]乙基三磷酸，一种新型的ATP发色和光亲和类似物。合成、表征及其与肌球蛋白亚片段1的相互作用。
Biochemistry. 1985 Sep 10;24(19):5226-35. doi: 10.1021/bi00340a041.
4
Photoaffinity labeling of skeletal myosin with 2-azidoadenosine triphosphate.用2-叠氮基三磷酸腺苷对骨骼肌肌球蛋白进行光亲和标记。
Biochemistry. 1993 Jun 8;32(22):5725-32. doi: 10.1021/bi00073a001.
5
Serine-324 of myosin's heavy chain is photoaffinity-labeled by 3'(2')-O-(4-benzoylbenzoyl)adenosine triphosphate.肌球蛋白重链的丝氨酸-324被3'（2'）-O-（4-苯甲酰苯甲酰基）三磷酸腺苷进行光亲和标记。
Biochemistry. 1989 May 2;28(9):3989-95. doi: 10.1021/bi00435a054.
6
Photoaffinity ADP analogs as covalently attached reporter groups of the active site of myosin subfragment 1.光亲和ADP类似物作为肌球蛋白亚片段1活性位点的共价连接报告基团。
Biochemistry. 1995 Feb 14;34(6):1978-87. doi: 10.1021/bi00006a019.
7
Photochemical probes of the active site of myosin. Irradiation of trapped 3'-O-(4-benzoyl)benzoyladenosine 5'-triphosphate labels the 50-kilodalton heavy chain tryptic peptide.肌球蛋白活性位点的光化学探针。对捕获的3'-O-(4-苯甲酰基)苯甲酰腺苷5'-三磷酸进行辐照，可标记50千道尔顿重链胰蛋白酶肽段。
J Biol Chem. 1984 Nov 10;259(21):12956-9.
8
2'-Deoxy-3'-O-(4-benzoylbenzoyl)- and 3'(2')-O-(4-benzoylbenzoyl)-1,N6-ethenoadenosine 5'-diphosphate, fluorescent photoaffinity analogues of adenosine 5'-diphosphate. Synthesis, characterization, and interaction with myosin subfragment 1.2'-脱氧-3'-O-(4-苯甲酰苯甲酰基)-和3'(2')-O-(4-苯甲酰苯甲酰基)-1,N6-乙烯腺苷5'-二磷酸，腺苷5'-二磷酸的荧光光亲和类似物。合成、表征及其与肌球蛋白亚片段1的相互作用。
Biochemistry. 1987 Nov 17;26(23):7524-34. doi: 10.1021/bi00397a048.
9
Direct chemical evidence that serine 180 in the glycine-rich loop of myosin binds to ATP.肌球蛋白富含甘氨酸环中丝氨酸180与ATP结合的直接化学证据。
J Biol Chem. 1989 Apr 25;264(12):6608-11.
10
Photolabeling evidence for calcium-induced conformational changes at the ATP binding site of scallop myosin.扇贝肌球蛋白ATP结合位点钙诱导构象变化的光标记证据
Proc Natl Acad Sci U S A. 1993 Jan 1;90(1):35-9. doi: 10.1073/pnas.90.1.35.

引用本文的文献

1
Conformational changes between the active-site and regulatory light chain of myosin as determined by luminescence resonance energy transfer: the effect of nucleotides and actin.通过发光共振能量转移测定的肌球蛋白活性位点与调节轻链之间的构象变化：核苷酸和肌动蛋白的影响。
Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15309-14. doi: 10.1073/pnas.95.26.15309.
2
Smooth muscle myosin mutants containing a single tryptophan reveal molecular interactions at the actin-binding interface.含有单个色氨酸的平滑肌肌球蛋白突变体揭示了肌动蛋白结合界面处的分子相互作用。
Proc Natl Acad Sci U S A. 1998 Oct 27;95(22):12944-9. doi: 10.1073/pnas.95.22.12944.
3
Photoaffinity labelling of smooth-muscle myosin by methylanthraniloyl-8-azido-ATP.用甲基邻氨基苯甲酰基-8-叠氮基-ATP对平滑肌肌球蛋白进行光亲和标记。
Biochem J. 1993 Jun 1;292 ( Pt 2)(Pt 2):439-44. doi: 10.1042/bj2920439.
4
Photolabeling evidence for calcium-induced conformational changes at the ATP binding site of scallop myosin.扇贝肌球蛋白ATP结合位点钙诱导构象变化的光标记证据
Proc Natl Acad Sci U S A. 1993 Jan 1;90(1):35-9. doi: 10.1073/pnas.90.1.35.
5
Synthesis of non-nucleotide ATP analogues and characterization of their chemomechanical interaction with muscle fibres.非核苷酸ATP类似物的合成及其与肌纤维化学机械相互作用的表征。
J Muscle Res Cell Motil. 1993 Oct;14(5):484-97. doi: 10.1007/BF00297211.
6
Cross-linking myosin subfragment 1 Cys-697 and Cys-707 modifies ATP and actin binding site interactions.交联肌球蛋白亚片段1的半胱氨酸-697和半胱氨酸-707会改变ATP与肌动蛋白结合位点的相互作用。
Biophys J. 1993 Sep;65(3):1121-9. doi: 10.1016/S0006-3495(93)81162-7.
7
Fluorescence studies on the nucleotide- and Ca2+-binding domains of molluscan myosin.软体动物肌球蛋白核苷酸结合域和钙离子结合域的荧光研究。
Biochem J. 1985 Oct 1;231(1):31-8. doi: 10.1042/bj2310031.
8
Conserved protein domains in a myosin heavy chain gene from Dictyostelium discoideum.盘基网柄菌肌球蛋白重链基因中的保守蛋白结构域。
Proc Natl Acad Sci U S A. 1986 Dec;83(24):9433-7. doi: 10.1073/pnas.83.24.9433.
9
The primary structure of the myosin head.肌球蛋白头部的一级结构。
Proc Natl Acad Sci U S A. 1987 Jan;84(2):416-20. doi: 10.1073/pnas.84.2.416.
10
Domains, motions and regulation in the myosin head.肌球蛋白头部的结构域、运动及调节
J Muscle Res Cell Motil. 1988 Aug;9(4):296-305. doi: 10.1007/BF01773873.

本文引用的文献

1
Chemical modification of myosin by active-site trapping of metal-nucleotides with thiol crosslinking reagents.通过用硫醇交联试剂对金属核苷酸进行活性位点捕获来对肌球蛋白进行化学修饰。
Methods Enzymol. 1982;85 Pt B:93-116. doi: 10.1016/0076-6879(82)85013-1.
2
Microsequence analysis of peptides and proteins. II. Separation of amino acid phenylthiohydantoin derivatives by high-performance liquid chromatography on octadecylsilane supports.肽与蛋白质的微量序列分析。II. 用十八烷基硅烷载体上的高效液相色谱法分离氨基酸苯硫代乙内酰脲衍生物
Anal Biochem. 1982 Mar 1;120(2):302-11. doi: 10.1016/0003-2697(82)90351-7.
3
Environment of the tryptophan residues in a myosin head: a hydrogen-deuterium exchange study.肌球蛋白头部色氨酸残基的环境：氢-氘交换研究
Biochemistry. 1981 Mar 3;20(5):1162-8. doi: 10.1021/bi00508a018.
4
Differences in chemical structure around the reactive lysine residues in the burst and the nonburst heads of skeletal muscle myosin.骨骼肌肌球蛋白爆发态头部和非爆发态头部中反应性赖氨酸残基周围化学结构的差异。
J Biochem. 1982 Jun;91(6):1845-53. doi: 10.1093/oxfordjournals.jbchem.a133881.
5
The sequence of the NH2-terminal 204-residue fragment of the heavy chain of rabbit skeletal muscle myosin.兔骨骼肌肌球蛋白重链氨基末端204个氨基酸残基片段的序列。
J Biol Chem. 1983 Nov 10;258(21):13100-10.
6
Protein structural domains in the Caenorhabditis elegans unc-54 myosin heavy chain gene are not separated by introns.秀丽隐杆线虫unc-54肌球蛋白重链基因中的蛋白质结构域未被内含子隔开。
Proc Natl Acad Sci U S A. 1983 Jul;80(14):4253-7. doi: 10.1073/pnas.80.14.4253.
7
Hydrolysis of ATP and reversible binding to F-actin by myosin heavy chains free of all light chains.肌球蛋白重链在不含所有轻链的情况下对ATP的水解以及与F-肌动蛋白的可逆结合。
Nature. 1981 Aug 6;292(5823):560-2. doi: 10.1038/292560a0.
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Regulation and kinetics of the actin-myosin-ATP interaction.肌动蛋白-肌球蛋白-ATP相互作用的调节与动力学
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9
Analysis of membranes photolabeled with lipid analogues. Reaction of phospholipids containing a disulfide group and a nitrene or carbene precursor with lipids and with gramicidin A.用脂质类似物进行光标记的膜的分析。含二硫基团以及氮烯或卡宾前体的磷脂与脂质及短杆菌肽A的反应。
J Biol Chem. 1980 Apr 25;255(8):3319-29.
10
The free heavy chain of vertebrate skeletal myosin subfragment 1 shows full enzymatic activity.脊椎动物骨骼肌肌球蛋白亚片段1的游离重链具有完整的酶活性。
J Biol Chem. 1982 Jan 25;257(2):1102-5.

用N-(4-叠氮基-2-硝基苯基)-2-氨基乙基二磷酸进行光亲和标记后鉴定骨骼肌肌球蛋白的活性位点肽段。

Identification of an active site peptide of skeletal myosin after photoaffinity labeling with N-(4-azido-2-nitrophenyl)-2-aminoethyl diphosphate.

作者信息

Okamoto Y, Yount R G

出版信息

Proc Natl Acad Sci U S A. 1985 Mar;82(6):1575-9. doi: 10.1073/pnas.82.6.1575.

DOI:10.1073/pnas.82.6.1575
PMID:3157189
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC397314/
Abstract

The active site of skeletal myosin has been photoaffinity labeled (approximately equal to 50%) by the ADP analog N-(4-azido-2-nitrophenyl)-2-aminoethyl triphosphate (NANDP) following the cobalt phenanthroline active site trapping procedure of Wells and Yount [Wells, J. A. & Yount, R. G. (1979) Proc. Natl. Acad. Sci. USA 76, 4966-4970]. Extensive proteolytic digestion of [3H]NANDP-labeled myosin subfragment one yielded two major peptides, P1 and P2, which were purified by reversed-phase high-performance liquid chromatography. These peptides represented 50% of all labeled amino acids and contained 1 mol of the unusual amino acid epsilon-N-trimethyllysine. Analysis of P2 by Edman techniques gave a sequence Val-Asn-Pro-Tyr-Lys(Me3)-X-Leu-Pro-Val-Tyr, which corresponds to an identical sequence for residues 125-134 determined by Tong and Elzinga [Tong, S. W. & Elzinga, M. (1983) J. Biol. Chem. 258, 13100-13110] for a segment of rabbit skeletal myosin heavy chain in which X is Trp-130. P1 was identical to P2 except it contained an additional three amino acids, Asn-Pro-Gln, at the COOH-terminal end. Amino acid composition, sequence data, spectral measurements, and location of radioactive label in both P1 and P2 all indicate Trp-130 is the major site of labeling by NANDP. The adjacent epsilon-N-trimethyllysine may provide part of the binding site for the triphosphate portion of ATP.

摘要

按照韦尔斯和扬特[韦尔斯，J. A. & 扬特，R. G.（1979年）《美国国家科学院院刊》76卷，4966 - 4970页]的钴菲咯啉活性位点捕获程序，骨骼肌肌球蛋白的活性位点已被ADP类似物N-(4-叠氮基-2-硝基苯基)-2-氨基乙基三磷酸（NANDP）光亲和标记（约50%）。对[³H]NANDP标记的肌球蛋白亚片段一进行广泛的蛋白酶消化，产生了两个主要肽段P1和P2，通过反相高效液相色谱法进行纯化。这些肽段占所有标记氨基酸的50%，并含有1摩尔不寻常的氨基酸ε-N-三甲基赖氨酸。通过埃德曼技术对P2进行分析，得到序列Val-Asn-Pro-Tyr-Lys(Me3)-X-Leu-Pro-Val-Tyr，这与汤和埃尔津加[汤，S. W. & 埃尔津加，M.（1983年）《生物化学杂志》258卷，13100 - 13110页]确定的兔骨骼肌肌球蛋白重链一段（其中X为Trp-130）的125 - 134位残基的相同序列相对应。P1与P2相同，只是在COOH末端含有另外三个氨基酸Asn-Pro-Gln。P1和P2的氨基酸组成、序列数据、光谱测量以及放射性标记的位置均表明Trp-130是NANDP标记的主要位点。相邻的ε-N-三甲基赖氨酸可能为ATP的三磷酸部分提供部分结合位点。