| 词条 | Peanut agglutinin |
| 释义 |
Peanut agglutinin (PNA) is plant lectin protein derived from the fruits of Arachis hypogaea. Peanut agglutinin may also be referred to as Arachis hypogaea lectin. Lectins recognise and bind particular sugar sequences in carbohydrates; peanut agglutinin binds the carbohydrate sequence Gal-β(1-3)-GalNAc. The name "peanut agglutinin" originates from its ability to stick together (agglutinate) cells, such as neuramidase-treated erythrocytes,[1] which have glycoproteins or glycolipids on their surface which include the Gal-β(1-3)-GalNAc carbohydrate sequence. Structure{{Infobox protein family| Symbol = Lectin_legB | Name = Legume lectin domain | image = PDB 1lem EBI.jpg | width = | caption = Structure of the monosaccharide binding site of lentil lectin.[2] | Pfam = PF00139 | Pfam_clan = CL0004 | InterPro = IPR001220 | SMART = | PROSITE = PDOC00278 | MEROPS = | SCOP = 1lem | TCDB = | OPM family = | OPM protein = | PDB = }} The protein is 273 amino acids in length with the first 23 residues acting and a signal peptide which is subsequently cleaved. It has a Uniprot accession of [https://www.uniprot.org/uniprot/P02872 P02872]. There are over 20 structures of this protein in the PDB which reveal and all beta-sheet protein with a tetrameric quaternary structure. It is a member of the Lectin_legB PFAM family. Available Structures of peanut agglutininUses in cell biology and biochemistryBecause peanut agglutinin specifically binds a particular carbohydrate sequence it finds use in a range of methods for cell biology and biochemistry. For example in PNA-affinity chromatography the binding specificity of peanut agglutinin is used to isolate glycosylated molecules which have the sugar sequence Gal-β(1-3)-GalNAc. Peanut agglutinin activity is inhibited by lactose and galactose which compete for the binding site. Other uses include:
See also
References1. ^{{cite web|publisher=|accessdate=2010-03-14|url=http://www.medicago.se/sites/default/files/pdf/productsheets/Arachis_Hypogaea_PNA_v._01.pdf|title=PNA specification sheet Medicago AB:|work=}}{{dead link|date=March 2018 |bot=InternetArchiveBot |fix-attempted=yes }} {{biochem-stub}}2. ^{{cite journal |vauthors=Loris R, Casset F, Bouckaert J, etal |title=The monosaccharide binding site of lentil lectin: an X-ray and molecular modelling study |journal=Glycoconj. J. |volume=11 |issue=6 |pages=507–17 |date=December 1994 |pmid=7696853 |doi= 10.1007/bf00731301|url=}} 3. ^{{cite journal|last1=Blumer|first1=Camile Garcia|last2=Restelli|first2=Adriana Ester|last3=Giudice|first3=Paula Toni Del|last4=Soler|first4=Thiesa Butterby|last5=Fraietta|first5=Renato|last6=Nichi|first6=Marcilio|last7=Bertolla|first7=Ricardo Pimenta|last8=Cedenho|first8=Agnaldo Pereira|title=Effect of varicocele on sperm function and semen oxidative stress|journal=BJU International|volume=109|issue=2|pages=259–265|doi=10.1111/j.1464-410X.2011.10240.x}} 4 : Plant lectins|Legume lectins|Glycoproteins|Peanuts |
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