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1
"Immunology", Src Homology 2 and Src Homology 3 Domains
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::2012/08/14::
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2
Protein folding of src SH3 domain by a Go model
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::2013/06/05::
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3
SH3 Dimerization
SH3 Dimerization
::2014/07/07::
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4
Sts-1
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::2013/03/28::
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Albania - przejazd drogą SH3. Trasa Elbasan - Librazhd - Qukes - Prrenjas - Qafe Thane.
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::2013/10/04::
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metadynamics in essential coordinates
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::2007/12/01::
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Henry Chang - The roles of Ack family kinases in Drosophila development
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::2013/10/25::
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Parkin E3 ubiquitin ligase
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::2013/09/19::
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9
SH3 trimer formation
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::2014/07/07::
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10
p21 activated protein kinase
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::2012/09/23::
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11
CASK / Lin-2 kinase domain (with sound)
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::2013/02/09::
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Top4 Jefes Terrorificos de los Video Juegos+Analisis SH3
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More Sh3 Problems
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::2013/07/17::
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14
SH3
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::2012/11/28::
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on ap lioa-lioa20kva SH3-lioa nhat linh 20kva 3pha 0913 839 600
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::2013/10/25::
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Sh3 foogy volumetric environment
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::2013/10/02::
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17
Seaking SH3 Biritsh Coast Guard landing at Den Helder Airport
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::2012/01/06::
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¡DESTRIPANDO PORTAVIONES!- Episodio 1- SH3- Biel40
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::2013/12/05::
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on ap lioa -lioa 20kva SH3 - lioa nhat linh 20kva 3pha- 0913 839 600
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on ap lioa 100kva- ổn áp 100kva SH3- ổn áp 100kva-lioa nhat linh 100kva 0913 839 600
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Introduction to Chemical Biology 128. Lecture 18. Terpenes and Cell Signaling, Part 2
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::2013/03/15::
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ALEX MAYER Монтаж SH3: Секреты
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::2013/09/17::
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BAR domain
BAR domain
::2013/01/24::
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::2009/06/05::
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Protein Kinase A vs. Kinase Domain in p150
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::2014/03/19::
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SH2 domain
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::2012/02/03::
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27
Kinase Domain of p150
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::2014/03/19::
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28
SH2 Domain Phosphotyrosine Capture Kits
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::2009/04/28::
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vinrar
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::2009/07/10::
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::2009/09/10::
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Introduction to Chemical Biology 128. Lecture 12. Protein Functions.
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::2013/02/19::
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::2014/02/01::
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::2008/10/31::
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Shining OS Version 1.2
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::2008/12/05::
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Sinking of HMS Barham 221029-06.mp4
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::2011/09/17::
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::2011/09/26::
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Victory at Sea Episode 4 Part 2
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::2011/08/09::
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::2011/07/02::
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Real-Time Multiscale Protein Folding Visualization
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RESULTS [51 .. 101]
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SH3 domain
1shg SH3 domain.png
Ribbon diagram of the SH3 domain, alpha spectrin, from chicken (PDB accession code 1SHG), colored from blue (N-terminus) to red (C-terminus).
Identifiers
Symbol SH3_1
Pfam PF00018
Pfam clan CL0010
InterPro IPR001452
SMART SM00326
PROSITE PS50002
SCOP 1shf
SUPERFAMILY 1shf
CDD cd00174

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.

Structure[edit]

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[edit]

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[edit]

See also[edit]

References[edit]

  1. ^ 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. 
  2. ^ Mayer BJ (April 2001). "SH3 domains: complexity in moderation". J. Cell. Sci. 114 (Pt 7): 1253–63. PMID 11256992. 
  3. ^ 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. 
  4. ^ 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. 
  5. ^ Pawson T (February 1995). "Protein modules and signalling networks". Nature 373 (6515): 573–80. doi:10.1038/373573a0. PMID 7531822. 
  6. ^ 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[edit]

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