SH3ドメイン、SH3領域、Src相同性領域3
- 関
- SH2 domain、Src homology domain
WordNet
- territory over which rule or control is exercised; "his domain extended into Europe"; "he made it the law of the land" (同)demesne, land
- (mathematics) the set of values of the independent variable for which a function is defined (同)domain of a function
- the 19th letter of the Roman alphabet (同)s
PrepTutorEJDIC
- (国の)領地,領土;(個人の)所有地 / (関心・活動などの)範囲,分野 / (個人・一族の)所有地 / (数学で)変域(関数の独立変数がとる値の集合)
- sulfurの化学記号 / {略}South[ern]
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/05/27 20:39:07」(JST)
[Wiki en表示]
| SH3 domain |
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Ribbon diagram of the SH3 domain, alpha spectrin, from chicken (PDB accession code 1SHG), colored from blue (N-terminus) to red (C-terminus).
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| Identifiers |
| Symbol |
SH3_1 |
| Pfam |
PF00018 |
| Pfam clan |
CL0010 |
| InterPro |
IPR001452 |
| SMART |
SM00326 |
| PROSITE |
PS50002 |
| SCOP |
1shf |
| SUPERFAMILY |
1shf |
| CDD |
cd00174 |
| Available protein structures: |
| Pfam |
structures |
| PDB |
RCSB PDB; PDBe; PDBj |
| PDBsum |
structure summary |
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The SRC Homology 3 Domain (or SH3 domain) is a small protein domain of about 60 amino acids residues first identified as a conserved sequence in the viral adaptor protein v-Crk and the non-catalytic parts of enzymes such as phospholipase and several cytoplasmic tyrosine kinases such as Abl and Src.[1][2] It has also been identified in several other protein families such as: PI3 Kinase, Ras GTPase-activating protein, CDC24 and cdc25.[3][4][5] SH3 domains are found in proteins of signaling pathways regulating the cytoskeleton, the Ras protein, and the Src kinase and many others. They also regulate the activity state of adaptor proteins and other tyrosine kinases and are thought to increase the substrate specificity of some tyrosine kinases by binding far away from the active site of the kinase. Approximately 300 SH3 domains are found in proteins encoded in the human genome.
Contents
- 1 Structure
- 2 Peptide binding
- 3 Proteins with SH3 domain
- 4 See also
- 5 References
- 6 External links
Structure
The SH3 domain has a characteristic beta-barrel fold that consists of five or six β-strands arranged as two tightly packed anti-parallel β sheets. The linker regions may contain short helices. The SH3-type fold is an ancient fold found in eukaryotes as well as prokaryotes.[6]
Peptide binding
The classical SH3 domain is usually found in proteins that interact with other proteins and mediate assembly of specific protein complexes, typically via binding to proline-rich peptides in their respective binding partner. Classical SH3 domains are restricted in humans to intracellular proteins, although the small human MIA family of extracellular proteins also contain a domain with an SH3-like fold.
Many SH3-binding epitopes of proteins have a consensus sequence that can be represented as a regular expression or Short linear motif:
-X-P-p-X-P-
1 2 3 4 5
with 1 and 4 being aliphatic amino acids, 2 and 5 always and 3 sometimes being proline. The sequence binds to the hydrophobic pocket of the SH3 domain. More recently, SH3 domains that bind to a core consensus motif R-x-x-K have been described. Examples are the C-terminal SH3 domains of adaptor proteins like Grb2 and Mona (a.k.a. Gads, Grap2, Grf40, GrpL etc.). Other SH3 binding motifs have emerged and are still emerging in the course of various molecular studies, highlighting the versatility of this domain.
Proteins with SH3 domain
- Adaptor proteins
- CDC24
- Cdc25
- PI3 kinase
- Phospholipase
- Ras GTPase-activating protein
- Vav proto-oncogene
- GRB2
- p54 S6 kinase 2 (S6K2)
- SH3D21
- C10orf76 (potentially)
- STAC3
- Some myosins
See also
- Src homology 2 domain-containing
- Structural domain
References
- ^ Pawson T, Schlessingert J (July 1993). "SH2 and SH3 domains". Curr. Biol. 3 (7): 434–42. doi:10.1016/0960-9822(93)90350-W. PMID 15335710.
- ^ Mayer BJ (April 2001). "SH3 domains: complexity in moderation". J. Cell. Sci. 114 (Pt 7): 1253–63. PMID 11256992.
- ^ Musacchio A, Gibson T, Lehto VP, Saraste M (July 1992). "SH3--an abundant protein domain in search of a function". FEBS Lett. 307 (1): 55–61. doi:10.1016/0014-5793(92)80901-R. PMID 1639195.
- ^ Mayer BJ, Baltimore D (January 1993). "Signalling through SH2 and SH3 domains". Trends Cell Biol. 3 (1): 8–13. doi:10.1016/0962-8924(93)90194-6. PMID 14731533.
- ^ Pawson T (February 1995). "Protein modules and signalling networks". Nature 373 (6515): 573–80. doi:10.1038/373573a0. PMID 7531822.
- ^ Whisstock JC, Lesk AM (April 1999). "SH3 domains in prokaryotes". Trends Biochem. Sci. 24 (4): 132–3. doi:10.1016/s0968-0004(99)01366-3. PMID 10322416.
External links
- Eukaryotic Linear Motif resource motif class LIG_SH3_1
- Eukaryotic Linear Motif resource motif class LIG_SH3_2
- Eukaryotic Linear Motif resource motif class LIG_SH3_3
- Eukaryotic Linear Motif resource motif class LIG_SH3_4
- Eukaryotic Linear Motif resource motif class LIG_SH3_5
- Eukaryotic Linear Motif resource motif class TRG_PEX_1
- Nash Lab Protein Interaction Domains in Signal Transduction - The SH3 domain
- GENEART - Screen your protein against all human SH3 domains in a single phage display cycle
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Protein domains
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- BAR
- BIR
- BZIP
- CARD
- C1
- C2
- DED
- ENTH
- FYVE
- HEAT
- Kringle
- LIM
- LRR
- NACHT
- PAS
- PDZ
- Pyrin
- PH
- PX
- SH2
- SH3
- SUN
- TRIO
- WD40
- zinc finger
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Index of genetics
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| Description |
- Gene expression
- DNA
- replication
- cycle
- recombination
- repair
- binding proteins
- Transcription
- factors
- regulators
- nucleic acids
- RNA
- RNA binding proteins
- ribonucleoproteins
- repeated sequence
- modification
- Translation
- ribosome
- modification
- nexins
- Proteins
- domains
- Structure
- primary
- secondary
- tertiary
- quaternary
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| Disease |
- Replication and repair
- Transcription factor
- Transcription
- Translation
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UpToDate Contents
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English Journal
- Isoform-specific roles of the GTPase activating protein Nadrin in cytoskeletal reorganization of platelets.
- Beck S, Fotinos A, Lang F, Gawaz M, Elvers M.SourceDepartment of Cardiology and Cardiovascular Medicine, University Clinic of Tübingen, Germany.
- Cellular signalling.Cell Signal.2013 Jan;25(1):236-46. doi: 10.1016/j.cellsig.2012.09.005. Epub 2012 Sep 10.
- Cytoskeletal reorganization of activated platelets plays a crucial role in hemostasis and thrombosis and implies activation of Rho GTPases. Rho GTPases are important regulators of cytoskeletal dynamics and function as molecular switches that cycle between an inactive and an active state. They are re
- PMID 22975681
- Abelson interactor-1 (ABI-1) interacts with MRL adaptor protein MIG-10 and is required in guided cell migrations and process outgrowth in C. elegans.
- McShea MA, Schmidt KL, Dubuke ML, Baldiga CE, Sullender ME, Reis AL, Zhang S, O'Toole SM, Jeffers MC, Warden RM, Kenney AH, Gosselin J, Kuhlwein M, Hashmi SK, Stringham EG, Ryder EF.SourceDepartment of Biology and Biotechnology, Worcester Polytechnic Institute, 100 Institute Road, Worcester, MA 01609, USA. Electronic address: momcshea@gmail.com.
- Developmental biology.Dev Biol.2013 Jan 1;373(1):1-13. doi: 10.1016/j.ydbio.2012.09.017. Epub 2012 Sep 27.
- Directed cell migration and process outgrowth are vital to proper development of many metazoan tissues. These processes are dependent on reorganization of the actin cytoskeleton in response to external guidance cues. During development of the nervous system, the MIG-10/RIAM/Lamellipodin (MRL) signal
- PMID 23022657
- Characterization of the Functional Domains of the SloR Metalloregulatory Protein in Streptococcus mutans.
- Haswell JR, Pruitt BW, Cornacchione LP, Coe CL, Smith EG, Spatafora GA.SourceMiddlebury College, Department of Biology, Middlebury, Vermont, USA.
- Journal of bacteriology.J Bacteriol.2013 Jan;195(1):126-34. doi: 10.1128/JB.01648-12. Epub 2012 Oct 26.
- Streptococcus mutans is a commensal member of the healthy plaque biofilm and the primary causative agent of dental caries. The present study is an investigation of SloR, a 25-kDa metalloregulatory protein that modulates genes responsible for S. mutans-induced cariogenesis. Previous studies of SloR h
- PMID 23104811
Japanese Journal
- 1PT157 Structural properties and folding process of hNck2 SH3 domain(The 50th Annual Meeting of the Biophysical Society of Japan)
- Matsumura Yoshitaka,Shinjo Masaji,Matsui Tsutomu,Ichimura Kaoru,Song Jianxing,Kihara Hiroshi
- 生物物理 52(SUPPLEMENT_1), S95, 2012-08-15
- NAID 110009584996
- 1PT115 Structural analysis of hNck2 SH3 domain at various pH : non-native α-helix-rich monomer and native dimer(The 50th Annual Meeting of the Biophysical Society of Japan)
- Shinjio Masaji,Matsumura Yoshitaka,Ichimura Kaoru,Song Jianxing,Kihara Hiroshi
- 生物物理 52(SUPPLEMENT_1), S88, 2012-08-15
- NAID 110009584954
- Genome-wide Investigation of the Rab Binding Activity of RUN Domains : Development of a Novel Tool that Specifically Traps GTP-Rab35
- Fukuda Mitsunori,Kobayashi Hotaka,Ishibashi Koutaro [他]
- Cell Structure and Function 36(1・2), 155-170, 2011-12-00
- NAID 40019163999
Related Links
- 米国CST社の日本法人CSTジャパン株式会社【公式サイト】プロリンリッチ配列の結合: SH3 ドメイン（領域）ページ。高品質の研究用試薬、米国本社の開発研究者による技術的サポートをご提供しております。
- 〈はじめに〉 SH3ドメインは、タンパク質のプロリンに富む領域と特異的に結合して、タンパク質－タンパク質間の相互作用を制御する機能ドメインであり、細胞内シグナル伝達に関与するタンパク質に広く見出されている。
★リンクテーブル★
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SH2ドメイン、SH2領域、Src相同性領域2
- 関
- SH3 domain、Src homology domain
[★]
- 英
- SH3 domain
- 関
- SH2領域、SH3領域、Src相同性領域、SH3ドメイン
[★]
- 関
- SH2 domain、SH3 domain
[★]
- 英
- SH3 domain
- 関
- Src相同性領域3、SH3ドメイン
[★]
- 同
- Src homology 3
- 同
- Src homology 3
[★]
- 関
- area、realm、region、regional、segregation、territory、universe
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- 関
- See also specific type