Sturdy Metal Stand Folds For Easy Storage Hinged Branches For Easy Assembly More product information 2 Buy on Tesco Direct from: Earn 20 Clubcard points Delivery options will be shown at checkout (or enable JavaScript to show on this page). We've carefully chosen all our Tesco Partners, to give you even more choice when you shop with us online. Browse a wider range of specialist products, all in one place Collect Clubcard points on every order Stay protected with the Tesco Partner Guarantee – we’re here to support you when buying from an approved Tesco Partner. Keep Christmas traditional this year with the Meribel green spruce tree. Made from high quality PVC with 500 tips, it will be the perfect festive addition to your home. The hinged branches make assembling the tree easy. Simply screw the stand together and slot in the tree sections. Once together the tree is sturdy and ready to separate out the branches and decorate. Remember to keep the box as the Meribel Spruce can be taken apart and placed to be stored year after year.
Base 16 inches, widest part of tree tip to tip 42 inches. Find where we are located View the Maps & Directions Page This content will open in a overlay Carlsbad, CA hotel overlooking beautiful Carlsbad Beach Indoor and outdoor Carlsbad meeting, event and wedding space for up to 400 guests 24-hour business center, fitness center and complimentary WiFi Complimentary WiFi and inviting guest rooms offering ocean views at your request The Carlsbad Beach Bistro, Pavilion Lounge, and 24-hour Pavilion Pantry® Breathtaking Ocean Vistas at this Carlsbad Beach Hotel Relax and recharge at the inviting Hilton Garden Inn Carlsbad Beach hotel. Situated within close walking distance of several Carlsbad beaches, this hotel offers breathtaking ocean views of the California coastline. Explore nearby San Diego area attractions such as LEGOLAND® California and San Diego Zoo. Located close to a range of local business headquarters, this Carlsbad, CA hotel boasts a large variety of versatile indoor and outdoor function space.
Host your dream wedding, special event or conference for up to 400 guests and enjoy professional planning advice. Stay productive in the 24-hour Business Center and keep in touch with complimentary WiFi throughout the hotel. Savor delicious California specialties at The Carlsbad Beach Bistro and unwind with cool, evening drinks and spectacular views on the ocean terrace. Enjoy the casual, welcoming surrounds of the Pavilion Lounge and snack on treats from the 24-hour Pavilion Pantry® convenience store. Feel invigorated with an energizing workout in the contemporary, 24-hour fitness center or plunge into the outdoor pool and whirlpool. Feel refreshed after a great night’s sleep in an inviting guest room, many with ocean views, and unwind with breathtaking vistas of Carlsbad Beach. Discover a variety of thoughtful conveniences including a microwave, refrigerator, and a coffeemaker. Stay connected with complimentary WiFi and enjoy a productive setting to catch up with work with the large desk, ergonomic chair and desk-level outlets.
Experience a successful stay at Hilton Garden Inn Carlsbad Beach in California, offering a choice of comforting and convenient facilities. Located near a number of local business headquarters, this Carlsbad hotel presents a huge range of diverse indoor and outdoor meeting space. Celebrate your dream wedding, special event or corporate meeting for up to 400 guests and relax while the professional catering and event staff take care of the details. Unwind with an evening drink at Pavilion Lounge or savor delicious Californian food at The Carlsbad Beach Bistro, and take in breathtaking ocean views from the fire-lit terrace. Re-energize in the modern 24-hour fitness center or plunge in to the outdoor pool with a whirlpool. Explore exciting San Diego-area attractions from the conveniently located Hilton Garden Inn Carlsbad Beach, situated just 30 minutes from downtown San Diego. Spend the day at San Diego Zoo or Sea World. Visit Carlsbad Flower Fields, explore downtown Carlsbad Village, or treat yourself at Carlsbad Premium Outlet Mall.
Enjoy a thrilling adventure at nearby LEGOLAND or unwind, surf, or jog on miles of stunning Carlsbad state beaches. Receive four (4), 2-day tickets along with breakfast for 4 Let us help plan your dream wedding in over 15,000 sq. ft. of beautiful indoor/outdoor ceremony space! Enjoy our proximity to Carlsbad Beach and spend a day in the sand with the family!The requested URL /Productlijnen/productlijn%20city.htm was not found on this server. ‘RNA recognition motifs (RRMs)’ are common domain‐folds composed of 80–90 amino‐acid residues in eukaryotes, and have been identified in many cellular proteins. At first they were known as RNA binding domains. Through discoveries over the past 20 years, however, the RRMs have been shown to exhibit versatile molecular recognition activities and to behave as molecular Lego building blocks to construct biological systems. Novel RNA/protein recognition modes by RRMs are being identified, and more information about the molecular recognition by RRMs is becoming available.
These RNA/protein recognition modes are strongly correlated with their biological significance. In this review, we would like to survey the recent progress on these versatileWIREs RNA 2012, 3:229–246. Schematic representation of the types of amino‐acid residues on the β‐sheet surfaces of RNA recognition motifs (RRMs). (a) Proportions of various amino‐acid residues on the β‐sheet surfaces of RRMs. The amino‐acid residues are shown for (b) TIA‐1 RRM2, (c) hTra2‐β, (d) p14, (e) Nup35, and (f) Prp24 RRM4. The aromatic amino‐acid residues and the Gly residue are colored red and cyan, respectively. The amino‐acid residues with side chains directed toward the inside of the RRM fold are colored light gray, and those with solvent‐exposed side chains are depicted in clear characters. In p14, Nup35, and Prp24 RRM4, the positions of the interacting amino‐acid residues are shown with the three‐letter code in a circle. The structures of the dimerized Nup35 RRM (PDB‐ID: 1WWH) and the Prp24 RRM4 (PDB‐ID: 2L9W) are demonstrated in the bottom panels of (e) and (f).
These figures were generated by the program MOLMOL.21 (g) The RRM structures are represented by one block for a single RRM (top) and two blocks for tandem RRMs (bottom). The well‐conserved β‐sheet surface corresponds to the top surface of the box. Each of the surfaces is numbered from 1 to 6. In addition, the N‐ and C‐terminal extensions are colored cyan and pink, respectively. In the case of the tandem RRMs, the surface numbers of the second RRM are underlined, and L indicates the linker between RRM1 and RRM2. Involvement of the N‐ and/or C‐terminal extension of the RNA recognition motif (RRM) in RNA recognition. (a) Structure of the U1A RRM1 in complex with stem II of the U1 snRNA (PDB‐ID: 1URN). (b) Structure of the CUG‐BP RRM3 in complex with 5′‐UGUGUG‐3′ (PDB‐ID: 2RQC). (c) Structure of the PTB RRM3 in complex with 5′‐UCUCU‐3′ (PDB‐ID: 2ADC). (d) Structure of the PTB RRM1 in complex with 5′‐CUCU‐3′ (PDB‐ID: 2AD9). (e) Structure of the hTra2‐β RRM in complex with 5′‐GAAGAA‐3′ (PDB‐ID: 2RRA).
(f) Structure of the C‐terminal RRM of the U11/U12‐65k protein (PDB‐ID: 3EGN). The β‐strands and α‐helices of the RRM body are colored cyan and orange, respectively. The N‐terminal extension that adopts the consecutive helical structure and holds the α2‐helix of the RRM body is colored pink. The U11/U12‐65k RRM contains an additional helical structure between the canonical α1–β2 loop. These figures were generated by the program MOLMOL.21 The appearance of the DxxT loop in RNA recognition motifs (RRMs). A total of 363 RRMs were aligned according to their homology to the TIA‐1 RRM2. (a) The RRMs containing the DxxT loop sequence are demonstrated by a red bar. If the appearance of the DxxT loops correlated well with the total sequence homology, then the DxxT loops were clustered in the high homology region, as seen in the assumptive data. (b) However, the actual data indicated that the appearance of the DxxT loop is discretely identified. RNA recognition on surfaces other than the β‐sheet.
(a) Poly(A)‐specific ribonuclease RNA recognition motifs (PARN RRM) in complex with the m7GpppG cap structure (PDB‐ID: 2ROK). (b) CBP20 in complex with the m7GpppG cap structure (PDB‐ID: 1H2T). (c) The MTHFSD RRM (PDB‐ID: 2E5J). (d) The hnRNP F RRM1 in complex with 5′‐AGGGAU‐3′ (PDB‐ID: 2KFY). In (a), (b), and (d), the aromatic amino‐acid residues that are involved in RNA recognition are colored orange, and those that interact with the N‐ and C‐terminal extensions are colored red. In addition, in (d), the charged amino‐acid residues involved in RNA binding are colored light green. In (c), a Trp residue is located at the position corresponding to the cap‐interacting Trp residue of the PARN RRM. However, this Trp residue is involved in core formation in the MTHFSD RRM, and is buried. Cooperativity between multi RRMs. (A) The Sxl RRM1–RRM2 in complex with 5′‐UGUUUUUUUU‐3′ (PDB‐ID: 1B7F). (b) The Hrp1 RRM1–RRM2 in complex with 5′‐UAUAUAU‐3′ (PDB‐ID: 2CJK).
(c) The PABP RRM1–RRM2 in complex with 5′‐AAAAAAAA‐3′ (PDB‐ID: 1CVJ). (d) The PTB RRM3–RRM4 in complex with PPT (poly‐pyrimidine tract) (PDB‐ID: 2EVZ). (e) Hrp1/Rna15 in complex with 5′‐UAUAUAUAAUAAU‐3′ (PDB‐ID: 2KM8). In (a) and (b), the key amino‐acid residues that stack with the starting nucleotide on RRM1 are colored magenta. In (e), the inset indicates an expanded region, demonstrating the putative electrostatic interactions between the Rna15 RRM and the Hrp1 RRM1. Comparison between HuD and CUG‐BP1. (a) HuD and CUG‐BP1 share a similar domain architecture, with two consecutive N‐terminal RRMs and a single C‐terminal RRM. The complex structure of HuD RRM1–RRM2 with its target RNA (PDB‐ID: 2FXL) and that of CUG‐BP1 RRM3 are shown. In addition, the complex structures of RRM1 and 2 of CUG‐BP1 with 5′‐UGUU‐3′ are demonstrated (PDB‐ID: 3NMR). These figures were generated by the program MOLMOL.21 The protein–RNA complex structures have been elucidated for all of them, except for the HuD C‐terminal RRM.
Models of the RNA binding modes of (B) HuC/D and (C) CUG‐BP1. Protein–protein interactions in the UHM‐type motif. (a) left: SPF45 (ribbon) with the KRKSRWDETP peptide (PDB‐ID: 2PEH). Right: SPF45 (surface) with the KRKSRWDETP peptide. (b) The eIF3b RRM (surface) with the DEDVKDNWDDD peptide (PDB‐ID: 2KRB). (c) The REF RRM (surface) with the ICP27 peptide (GPLGSVWSRLGARRPSCSP) (PDB‐ID: 2KT5). In this figure, only the underlined regions are depicted. In all of the peptide presentations, the side chains of the positively charged, negatively charged, and hydrophobic amino‐acid residues are colored blue, red and grey, respectively. Protein–protein interactions on the β‐sheet surface. (a) The p14 RRM with the SF3b155 fragment: the main chains of p14 RRM (pink) with the SF3b155 fragment (blue) are demonstrated (PDB‐ID: 3LQV). The aromatic side chain of p14 and the SF3b155 peptide are colored grey and purple, respectively. The co‐crystallized adenine base is located on RNP2, and is colored pale green.
(a) The RRM of the Cyp33 protein with the peptide fragment of the MLL onco‐protein (PDB‐ID: 2KV7). The main chains of the CYp33 RRM and MLL proteins are colored orange and deep pink, respectively. In addition, their side chains are colored green and magenta, respectively. (a) Dimeric structure of the XePABP2 RRM (PDB‐ID: 2JWN). The β‐strands of each unit are colored blue and cyan, respectively. Correspondingly, the α‐helical regions are colored pink and red. The β2‐strands of each unit are paired with each other in an antiparallel manner. (b) The complex structure of FIR RRM1‐2 and the N‐box peptide of the FBP protein (PDB‐ID: 2KXH). The FIR RRM1, RRM2, and the N‐box peptide are colored pale green, blue, and deep pink, respectively. Protein–protein interactions involving regions other than the β‐sheet surface and the α‐helix. (a) The CFIm25/CFIm68 RRM with the target RNA (PDB‐ID: 3P6Y). (b) The SF2 RRM2 and SRPK1 (PDB‐ID: 3BEJ). (c) The Raver protein with the Vinculin tail domain (PDB‐ID: 3H2U).