59:
135:. In spite of serine and threonine having one less sidechain atom, such that the sidechain-mainchain mimicry of β turns is imperfect, these features occur in proteins as the four types in numbers approaching those of Asx turns. They also exhibit a tendency to substitute each other over evolutionary time.
62:
An Asx turn with an aspartate at residue i. One of the sidechain oxygens of the aspartate forms a hydrogen bond (dotted line) with the mainchain NH group of residue i+2. Colors: red, oxygen; grey, carbon; blue, nitrogen. Hydrogen atoms are
75:
have structurally similar hydrogen-bonded loops and exhibit sidechain-mainchain mimicry in the sense that the sidechain of residue i of the Asx turn mimics the mainchain of residue i of the
729:
Wan, W-Y; Milner-White EJ (2009). "A Recurring Two-Hydrogen-bond Motif
Incorporating a Serine or Threonine Residue is found both at α-Helical N Termini and in Other Situations".
404:
Thakur, AK; Kishore R (2006). "Characterization of β-turn and asx-turns mimicry in a model peptide : Stabilization via C-H•••O interaction".
67:
Four types of Asx turn can be distinguished: types I, I’, II and II’. These categories correspond to those of the better-known hydrogen-bonded
47:
from its sidechain CO group to the mainchain NH group of residue i+2. About 14% of Asx residues present in proteins belong to Asx turns.
901:
175:
637:
Gunasekaran, K; Nagarajam HA; Ramakrishnan, C; Balaram, P (1998). "Stereochemical punctuation marks in protein structure".
71:, which have four residues and a hydrogen bond between the CO of residue i and the NH of residue i+3. Asx turns and
138:
A proportion of Asx turns are accompanied by a mainchain–mainchain hydrogen bond that qualifies them as
275:"Secondary structures without backbone: An analysis of backbone mimicry by polar side chains in proteins"
50:
The name "Asx" is used here to represent either of the amino acids aspartate (Asp) or asparagine (Asn).
554:
200:
238:
Rees, DC; Lewis M (1983). "Refined crystal structure of carboxypeptidase a at 1.54 Å resolution".
79:. Regarding their occurrence in proteins, they differ in that type I is the commonest of the four
662:
429:
203:(1982). "Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase".
878:
827:
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212:
163:
796:"Motivated Proteins: A web application for studying small three-dimensional protein motifs"
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167:
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216:
44:
666:
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28:
100:
58:
291:
274:
449:"Mimicry by asx- and ST-turns of the four main types of beta turn in proteins"
40:
32:
863:
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566:
139:
128:
104:
96:
80:
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72:
68:
36:
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682:"Mimicry by asx- and ST-turns of the four main types of β-turn in proteins"
650:
605:
513:
482:
425:
390:
357:"Mimicry by asx- and ST-turns of the four main types of β-turn in proteins"
341:
316:"Interrelationships of side-chain and main-chain conformations in proteins"
300:
776:
766:
658:
623:
574:
531:
496:
Doig, AJ; Macarthur MW; MacArthur, Malcolm W.; Thornton, Janet M. (1997).
259:
224:
185:
108:
24:
697:
680:
Duddy, WJ; Nissink WMJ; Allen, Frank H.; Milner-White, E. James (2004).
464:
447:
Duddy, WJ; Nissink WMJ; Allen, Frank H.; Milner-White, E. James (2004).
372:
355:
Duddy, WJ; Nissink WMJ; Allen, Frank H.; Milner-White, E. James (2004).
158:
Richardson, JS (1981). "The anatomy and taxonomy of protein structure".
132:
92:
417:
124:
112:
57:
115:
residue. They are thus often regarded as helix capping features.
35:
residues (labeled i, i+1 and i+2) in which residue i is an
83:while type II’ is the commonest of the Asx turns.
498:"Structures of N-termini of helices in proteins"
847:"MSDmotif: exploring protein sites and motifs"
111:such that the Asx, serine or threonine is the
8:
320:Progress in Biophysics and Molecular Biology
545:Presta, LG; Rose GD (1988). "Helix Caps".
872:
862:
821:
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705:
613:
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786:
160:Advances in Protein Chemistry Volume 34
150:
7:
794:Leader, DP; Milner-White EJ (2009).
16:Feature in proteins and polypeptides
162:. Vol. 34. pp. 167–339.
14:
273:Eswar, N; Ramachandran C (1999).
131:as residue i, which are called
845:Golovin, A; Henrick K (2008).
314:Chakrabarti, P; Pal D (2001).
1:
333:10.1016/s0079-6107(01)00005-0
252:10.1016/S0022-2836(83)80024-2
168:10.1016/S0065-3233(08)60520-3
95:both occur frequently at the
731:Journal of Molecular Biology
639:Journal of Molecular Biology
240:Journal of Molecular Biology
217:10.1016/0022-2836(82)90174-7
205:Journal of Molecular Biology
588:Aurora, R; Rose GD (1998).
23:is a structural feature in
918:
123:Similar motifs occur with
902:Protein structural motifs
292:10.1093/protein/12.6.447
864:10.1186/1471-2105-9-312
813:10.1186/1471-2105-10-60
567:10.1126/science.2837824
31:. It consists of three
743:10.1006/jmbi.1999.2551
651:10.1006/jmbi.1997.1505
606:10.1002/pro.5560070103
514:10.1002/pro.5560060117
64:
61:
698:10.1110/ps.04920904
559:1988Sci...240.1632P
553:(4859): 1632–1641.
465:10.1110/ps.04920904
373:10.1110/ps.04920904
279:Protein Engineering
43:(Asn) that forms a
851:BMC Bioinformatics
800:BMC Bioinformatics
767:Motivated Proteins
65:
692:(11): 3051–3055.
459:(11): 3051–3055.
418:10.1002/bip.20441
367:(11): 3051–3055.
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686:Protein Science
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594:Protein Science
590:"Helix Capping"
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502:Protein Science
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761:External links
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645:(5): 917–932.
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508:(1): 147–155.
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412:(6): 440–449.
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326:(1–2): 1–102.
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246:(2): 367–387.
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211:(2): 181–217.
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119:Related motifs
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45:hydrogen bond
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600:(1): 21–38.
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29:polypeptides
20:
18:
406:Biopolymers
201:Getzoff ED
146:References
140:Asx motifs
105:Asx motifs
87:Occurrence
81:beta turns
73:beta turns
69:beta turns
41:asparagine
33:amino acid
772:PDBeMotif
129:threonine
109:ST motifs
101:α-helices
97:N-termini
77:beta turn
39:(Asp) or
37:aspartate
896:Category
883:18637174
832:19210785
751:10064721
716:15459339
667:35919397
483:15459339
434:27091571
426:16411188
391:15459339
342:11389934
301:10388841
133:ST turns
93:ST turns
91:Asx and
63:omitted.
25:proteins
21:Asx turn
874:2491636
857:: 312.
823:2651126
707:2286581
659:9480777
624:9514257
615:2143812
575:2837824
555:Bibcode
547:Science
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523:2143508
474:2286581
382:2286581
260:6887246
225:7175933
186:7020376
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125:serine
663:S2CID
430:S2CID
113:N cap
54:Types
879:PMID
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712:PMID
655:PMID
620:PMID
571:PMID
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338:PMID
297:PMID
256:PMID
221:PMID
182:PMID
172:ISBN
27:and
19:The
869:PMC
859:doi
818:PMC
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739:doi
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