Knowledge (XXG)

Binding domain

Source 📝

358: 151:
Yong, J., T. J. Golembe, D. J. Battle, L. Pellizzoni, and G. Dreyfuss. "SnRNAs Contain Specific SMN-binding Domains That Are Essential for SnRNP Assembly".
183: 74:. Binding domains are essential for the function of many proteins. They are essential because they help splice, assemble, and translate proteins. 399: 211: 176: 392: 70:, function, and live by itself independent of the rest of the protein chain. Upon binding, proteins may undergo a 63: 418: 169: 99: 423: 385: 315: 71: 206: 47: 43: 94: 247: 221: 135: 31: 369: 325: 283: 278: 273: 127: 59: 231: 216: 252: 39: 131: 412: 310: 305: 330: 320: 78: 118:
Phillips, DC. (1966). "The three-dimensional structure of an enzyme molecule".
17: 257: 335: 67: 27:
Region of a protein which can bind to biomolecules with chemical specificity
139: 288: 226: 365: 298: 293: 192: 82: 51: 357: 155:. U.S. National Library of Medicine, April 2004. Retrieved April 2017. 165: 55: 161: 373: 266: 240: 199: 393: 177: 8: 400: 386: 184: 170: 162: 77:Examples of binding domains include the 111: 7: 354: 352: 58:. A protein domain is a part of a 372:. You can help Knowledge (XXG) by 25: 132:10.1038/scientificamerican1166-78 356: 212:Post-translational modification 153:Molecular and Cellular Biology 1: 440: 351: 253:Protein structural domains 85:, which binds to calcium. 81:, which binds to DNA, and 50:atom or molecule, such as 100:Receptor (biochemistry) 368:-related article is a 316:Photoreceptor protein 72:conformational change 207:Protein biosynthesis 120:Scientific American 95:DNA-binding domain 64:tertiary structure 381: 380: 346: 345: 248:Protein structure 222:Protein targeting 32:molecular biology 16:(Redirected from 431: 402: 395: 388: 360: 353: 326:Phycobiliprotein 284:Globular protein 279:Membrane protein 274:List of proteins 186: 179: 172: 163: 156: 149: 143: 116: 68:change or evolve 60:protein sequence 21: 439: 438: 434: 433: 432: 430: 429: 428: 419:Protein domains 409: 408: 407: 406: 349: 347: 342: 306:Fibrous protein 262: 236: 232:Protein methods 217:Protein folding 195: 190: 160: 159: 150: 146: 117: 113: 108: 91: 28: 23: 22: 18:Binding domains 15: 12: 11: 5: 437: 435: 427: 426: 421: 411: 410: 405: 404: 397: 390: 382: 379: 378: 361: 344: 343: 341: 340: 339: 338: 333: 328: 318: 313: 308: 303: 302: 301: 296: 291: 281: 276: 270: 268: 264: 263: 261: 260: 255: 250: 244: 242: 238: 237: 235: 234: 229: 224: 219: 214: 209: 203: 201: 197: 196: 191: 189: 188: 181: 174: 166: 158: 157: 144: 110: 109: 107: 104: 103: 102: 97: 90: 87: 40:protein domain 36:binding domain 26: 24: 14: 13: 10: 9: 6: 4: 3: 2: 436: 425: 424:Protein stubs 422: 420: 417: 416: 414: 403: 398: 396: 391: 389: 384: 383: 377: 375: 371: 367: 362: 359: 355: 350: 337: 334: 332: 329: 327: 324: 323: 322: 319: 317: 314: 312: 311:Chromoprotein 309: 307: 304: 300: 297: 295: 292: 290: 287: 286: 285: 282: 280: 277: 275: 272: 271: 269: 265: 259: 256: 254: 251: 249: 246: 245: 243: 239: 233: 230: 228: 225: 223: 220: 218: 215: 213: 210: 208: 205: 204: 202: 198: 194: 187: 182: 180: 175: 173: 168: 167: 164: 154: 148: 145: 141: 137: 133: 129: 125: 121: 115: 112: 105: 101: 98: 96: 93: 92: 88: 86: 84: 80: 75: 73: 69: 65: 61: 57: 53: 49: 45: 41: 37: 33: 19: 374:expanding it 363: 348: 152: 147: 126:(5): 78–90. 123: 119: 114: 76: 35: 29: 331:Phytochrome 321:Biliprotein 79:Zinc finger 413:Categories 258:Proteasome 241:Structures 106:References 336:Lipocalin 200:Processes 66:that can 289:Globulin 227:Proteome 193:Proteins 89:See also 48:specific 366:protein 299:Albumin 294:Edestin 140:5978599 83:EF hand 52:calcium 138:  62:and a 42:which 364:This 267:Types 46:to a 44:binds 38:is a 370:stub 136:PMID 128:doi 124:215 56:DNA 54:or 30:In 415:: 134:. 122:. 34:, 401:e 394:t 387:v 376:. 185:e 178:t 171:v 142:. 130:: 20:)

Index

Binding domains
molecular biology
protein domain
binds
specific
calcium
DNA
protein sequence
tertiary structure
change or evolve
conformational change
Zinc finger
EF hand
DNA-binding domain
Receptor (biochemistry)
doi
10.1038/scientificamerican1166-78
PMID
5978599
v
t
e
Proteins
Protein biosynthesis
Post-translational modification
Protein folding
Protein targeting
Proteome
Protein methods
Protein structure

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