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Protein dimer

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Sluis-Cremer N, Hamamouch N, San Félix A, Velazquez S, Balzarini J, Camarasa MJ (August 2006). "Structure-activity relationships of - 3'-spiro-5' '-(4' '-amino-1' ',2' '-oxathiole-2' ',2' '-dioxide)thymine derivatives as inhibitors of HIV-1 reverse transcriptase dimerization".
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versions of alkaline phosphatase were combined, the heterodimeric enzymes formed as a result exhibited a higher level of activity than would be expected based on the relative activities of the parental enzymes. These findings indicated that the dimer structure of the
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Cartoon diagram of a dimer of Escherichia coli galactose-1-phosphate uridylyltransferase (GALT) in complex with UDP-galactose (stick models). Potassium, zinc, and iron ions are visible as purple, gray, and bronze-colored spheres
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Filipiuc, Leontina Elena; Ababei, Daniela Carmen; Alexa-Stratulat, Teodora; Pricope, Cosmin Vasilica; Bild, Veronica; Stefanescu, Raluca; Stanciu, Gabriela Dumitrita; Tamba, Bogdan-Ionel (2021-11-01).
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Hehir, Michael J.; Murphy, Jennifer E.; Kantrowitz, Evan R. (2000). "Characterization of Heterodimeric Alkaline Phosphatases from Escherichia coli: An Investigation of Intragenic Complementation".
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8. Hjorleifsson, Jens GuMundur, and Bjarni Asgeirsson. “Cold-Active Alkaline Phosphatase Is Irreversibly Transformed into an Inactive Dimer by Low Urea Concentrations.”
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Amoutzias, Grigoris D.; Robertson, David L.; Van de Peer, Yves; Oliver, Stephen G. (2008-05-01). "Choose your partners: dimerization in eukaryotic transcription factors".
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alkaline phosphatase allows cooperative interactions between the constituent mutant monomers that can generate a more functional form of the
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Herscovitch M, Comb W, Ennis T, Coleman K, Yong S, Armstead B, Kalaitzidis D, Chandani S, Gilmore TD (February 2008).
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Some proteins contain specialized domains to ensure dimerization (dimerization domains) and specificity.
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have the ability to form both homo- and heterodimers with several types of receptors such as
537: 500: 482: 435: 398: 390: 351: 221: 193: 118: 48: 578:, vol. 1864, no. 7, 2016, pp. 755–765, https://doi.org/10.1016/j.bbapap.2016.03.016. 596: 505: 470: 403: 378: 311: 172: 164: 606: 379:"Intermolecular disulfide bond formation in the NEMO dimer requires Cys54 and Cys347" 297:. The dimer has two active sites, each containing two zinc ions and a magnesium ion. 106: 56: 562:
G protein coupled receptors modeling, activation, interactions and virtual screening
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Macromolecular complex formed by two, usually non-covalently bound, macromolecules
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formed by two protein monomers, or single proteins, which are usually
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Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
109:. An example of a non-covalent heterodimer is the enzyme 105:
Most protein dimers in biochemistry are not connected by
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Protein Dimerization and Oligomerization in Biology
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Biochemical and Biophysical Research Communications
117:chains. An exception is dimers that are linked by 8: 504: 486: 402: 587: 333: 113:, which is composed of two different 102:is formed by two different proteins. 7: 25: 590: 121:such as the homodimeric protein 83:. A protein dimer is a type of 71:has roots meaning "two parts", 47:is a macromolecular complex or 428:Trends in Biochemical Sciences 178:Variable surface glycoproteins 1: 488:10.3390/pharmaceutics13111823 530:Journal of Molecular Biology 284:. That is, when particular 85:protein quaternary structure 571:. Springer New York, 2012. 567:7. Matthews, Jacqueline M. 564:(1st ed.). Academic Press. 280:, a dimer enzyme, exhibits 251:Type II restriction enzymes 94:is formed by two identical 639: 440:10.1016/j.tibs.2008.02.002 395:10.1016/j.bbrc.2007.12.123 282:intragenic complementation 238:Receptor tyrosine kinases 256:Triosephosphateisomerase 67:, form dimers. The word 542:10.1006/jmbi.2000.4230 36: 262:Alcohol dehydrogenase 160:Transcription factors 136:cannabinoid receptors 111:reverse transcriptase 33: 278:alkaline phosphatase 270:Alkaline phosphatase 53:non-covalently bound 618:Dimers (chemistry) 233:Toll-like receptor 37: 623:Protein complexes 613:Protein structure 560:6. Conn. (2013). 356:10.1021/jm0604575 307:Dimer (chemistry) 222:Nuclear receptors 133:G protein-coupled 119:disulfide bridges 16:(Redirected from 630: 595: 594: 586: 554: 553: 525: 519: 518: 508: 490: 466: 460: 459: 423: 417: 416: 406: 374: 368: 367: 338: 229:βγ-subunit dimer 194:clotting factors 98:while a protein 21: 638: 637: 633: 632: 631: 629: 628: 627: 603: 602: 601: 589: 581: 558: 557: 527: 526: 522: 468: 467: 463: 425: 424: 420: 376: 375: 371: 350:(16): 4834–41. 340: 339: 335: 330: 303: 272: 173:14-3-3 proteins 156: 28: 23: 22: 15: 12: 11: 5: 636: 634: 626: 625: 620: 615: 605: 604: 600: 599: 556: 555: 536:(4): 645–656. 520: 461: 434:(5): 220–229. 418: 369: 332: 331: 329: 326: 325: 324: 319: 314: 312:Protein trimer 309: 302: 299: 271: 268: 267: 266: 265: 264: 259: 253: 242: 241: 240: 235: 230: 224: 213: 212: 211: 206: 201: 190: 185: 175: 170: 169: 168: 167:motif proteins 165:Leucine zipper 155: 152: 107:covalent bonds 57:macromolecules 26: 24: 14: 13: 10: 9: 6: 4: 3: 2: 635: 624: 621: 619: 616: 614: 611: 610: 608: 598: 593: 588: 584: 579: 577: 572: 570: 565: 563: 551: 547: 543: 539: 535: 531: 524: 521: 516: 512: 507: 502: 498: 494: 489: 484: 480: 476: 475:Pharmaceutics 472: 465: 462: 457: 453: 449: 445: 441: 437: 433: 429: 422: 419: 414: 410: 405: 400: 396: 392: 388: 384: 380: 373: 370: 365: 361: 357: 353: 349: 345: 337: 334: 327: 323: 320: 318: 315: 313: 310: 308: 305: 304: 300: 298: 296: 292: 287: 283: 279: 276: 269: 263: 260: 257: 254: 252: 249: 248: 247: 243: 239: 236: 234: 231: 228: 225: 223: 220: 219: 218: 214: 210: 207: 205: 202: 200: 197: 196: 195: 191: 189: 186: 183: 179: 176: 174: 171: 166: 163: 162: 161: 158: 157: 153: 151: 149: 145: 141: 137: 134: 129: 126: 124: 120: 116: 112: 108: 103: 101: 97: 93: 88: 86: 82: 81: 76: 75: 70: 66: 65:nucleic acids 62: 58: 54: 50: 46: 45:protein dimer 42: 35:respectively. 32: 19: 575: 573: 568: 566: 561: 559: 533: 529: 523: 481:(11): 1823. 478: 474: 464: 431: 427: 421: 389:(1): 103–8. 386: 382: 372: 347: 344:J. Med. Chem 343: 336: 290: 274: 273: 181: 148:adenosine A2 130: 127: 104: 99: 91: 89: 78: 72: 68: 44: 41:biochemistry 38: 204:Factor XIII 182:Trypanosoma 150:receptors. 100:heterodimer 607:Categories 328:References 295:holoenzyme 209:Fibrinogen 115:amino acid 90:A protein 59:, such as 18:Homodimers 497:1999-4923 448:0968-0004 227:G protein 217:receptors 199:Factor XI 140:mu-opioid 92:homodimer 550:11099386 515:34834237 456:18406148 413:18164680 364:16884295 317:Oligomer 301:See also 184:parasite 154:Examples 144:dopamine 96:proteins 61:proteins 49:multimer 597:Biology 506:8625816 404:2277332 322:ProtCID 291:E. coli 275:E. coli 246:enzymes 188:Tubulin 180:of the 55:. Many 583:Portal 548:  513:  503:  495:  454:  446:  411:  401:  362:  286:mutant 258:(TIM) 244:Some 215:Some 192:Some 69:dimer 546:PMID 511:PMID 493:ISSN 452:PMID 444:ISSN 409:PMID 360:PMID 146:and 131:The 123:NEMO 80:-mer 43:, a 538:doi 534:304 501:PMC 483:doi 436:doi 399:PMC 391:doi 387:367 352:doi 74:di- 63:or 39:In 609:: 544:. 532:. 509:. 499:. 491:. 479:13 477:. 473:. 450:. 442:. 432:33 430:. 407:. 397:. 385:. 381:. 358:. 348:49 346:. 142:, 125:. 87:. 77:+ 585:: 552:. 540:: 517:. 485:: 458:. 438:: 415:. 393:: 366:. 354:: 20:)

Index

Homodimers

biochemistry
multimer
non-covalently bound
macromolecules
proteins
nucleic acids
di-
-mer
protein quaternary structure
proteins
covalent bonds
reverse transcriptase
amino acid
disulfide bridges
NEMO
G protein-coupled
cannabinoid receptors
mu-opioid
dopamine
adenosine A2
Transcription factors
Leucine zipper
14-3-3 proteins
Variable surface glycoproteins
Tubulin
clotting factors
Factor XI
Factor XIII

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