1i16
From Proteopedia
STRUCTURE OF INTERLEUKIN 16: IMPLICATIONS FOR FUNCTION, NMR, 20 STRUCTURES
Structural highlights
FunctionIL16_HUMAN Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4.[1] [2] Isoform 1 may act as a scaffolding protein that anchors ion channels in the membrane.[3] [4] Isoform 3 is involved in cell cycle progression in T-cells. Appears to be involved in transcriptional regulation of SKP2 and is probably part of a transcriptional repression complex on the core promoter of the SKP2 gene. May act as a scaffold for GABPB1 (the DNA-binding subunit the GABP transcription factor complex) and HDAC3 thus maintaining transcriptional repression and blocking cell cycle progression in resting T-cells.[5] [6] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of a folded core of IL-16 is similar to that of intracellular protein modules called PDZ domains. IL-16 is thus the first extracellular protein found to have a PDZ-like fold. However, it does not exhibit normal peptide binding properties of PDZ domains. This is due to alterations of the structure at the 'PDZ-like binding site' of IL-16 (the GLGF cleft): the GLGF cleft of IL-16 is much smaller than those of PDZ-domains and is additionally blocked with a tryptophan side chain at its center. Our experiments indicate also that IL-16 nonspecifically aggregates in solution; but formation of a homo-tetrameric protein is not required, in contrast to previous suggestions, for its chemo-attractant activity. Structure of interleukin 16 resembles a PDZ domain with an occluded peptide binding site.,Muhlhahn P, Zweckstetter M, Georgescu J, Ciosto C, Renner C, Lanzendorfer M, Lang K, Ambrosius D, Baier M, Kurth R, Holak TA Nat Struct Biol. 1998 Aug;5(8):682-6. PMID:9699630[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Homo sapiens | Large Structures | Ambrosius D | Baier M | Ciosto C | Georgescu J | Holak TA | Kurth R | Lang K | Lanzendoerfer M | Muehlhahn P | Renner C | Zweckstetter M
