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Immunoglobulin I-set domain

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Immunoglobulin I-set domain
Structures of fibroblast growth factor 1.[1]
Identifiers
SymbolI-set
PfamPF07679
InterProIPR013098
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1bihB:327-412 1cs6A:322-407 1cvsC:159-247 1epfB:20-114 1evtD:159-247 1fhgA:42-132 1fq9C:159-247 1gxeA:652-767 1ie5A:214-304 1ij9A:25-112 1koa:6585-6674 1pd6A:363-448 1qctE:153-241 1qz1A:214-305 1ry7B:157-245 1tlk:42-132 1tnm:33489-3357 1tnn:33489-3357 1u2hA:43-113 1vcaA:25-112 1vscA:25-112 1wf5A:306-320 1wit:4150-4239 1wiu:4150-4239 1wwcA:325-352 1x44A:342-430 2cqvA:1238-1327 2cryA:419-516 2ncm:20-114

I-set domains are found in several cell adhesion molecules, including vascular (VCAM), intercellular (ICAM), neural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules, as well as junction adhesion molecules (JAM). I-set domains are also present in several other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1,[2] and the signalling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.[3]

Human proteins containing this domain

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References

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  1. ^ Plotnikov AN, Hubbard SR, Schlessinger J, Mohammadi M (May 2000). "Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity". Cell. 101 (4): 413–24. doi:10.1016/S0092-8674(00)80851-X. PMID 10830168. S2CID 16374022.
  2. ^ Sonderegger P, Welte W, Diederichs K, Freigang J, Proba K, Leder L (2000). "The crystal structure of the ligand binding module of axonin-1/TAG-1 suggests a zipper mechanism for neural cell adhesion" (PDF). Cell. 101 (4): 425–33. doi:10.1016/S0092-8674(00)80852-1. PMID 10830169. S2CID 15440572. Archived from the original (PDF) on 2018-07-19. Retrieved 2020-09-03.
  3. ^ Stuart DI, Jones EY, Harlos K, Esnouf RM, Love CA (2006). "Structure determination of human semaphorin 4D as an example of the use of MAD in non-optimal cases". Acta Crystallogr. D. 62 (Pt 1): 108–15. doi:10.1107/S0907444905034992. PMID 16369100.
This article incorporates text from the public domain Pfam and InterPro: IPR013098