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InterPro: IPR013106 Immunoglobulin V-set

Protein matches Help

UniProtKB

Matches:

5986 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR013106 Ig_V-set

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF07686	V-set	5986
Signatures in BioMart

InterPro Relationships Help

Children

IPR003596 Immunoglobulin V-set, subgroup
IPR013285 T-cell surface antigen CD2

Found in

IPR000920 Myelin P0 protein
IPR003989 Vascular cell adhesion molecule-1
IPR007110 Immunoglobulin-like
IPR008096 Cytotoxic T-lymphocyte antigen 4
IPR009136 Tyrosine-protein kinase, vascular endothelial growth factor receptor 2 (VEGFR2)
IPR015468 CD8 alpha subunit
IPR020718 Tyrosine-protein kinase, PDGF/VEGF receptor, fly
IPR020721 Tyrosine-protein kinase, vascular endothelial growth factor receptor 3 (VEGFR3)
IPR020729 Tyrosine-protein kinase, macrophage colony-stimulating factor 1 receptor
IPR020732 Tyrosine-protein kinase, fibroblast growth factor receptor-related

Contains

IPR003599 Immunoglobulin subtype

InterPro annotation

Entry Details in BioMart

Abstract

The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulphide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha, delta, epsilon, gamma and mu, all consisting of a variable domain (VH) and three (in alpha, delta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins, in which the variable and constant domains have clear, conserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; IPR013106), C1-set (constant-1; IPR003597), C2-set (constant-2; IPR008424) and I-set (intermediate; IPR013098) [1]. Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure, with the types differing in the number of strands in the beta-sheets as well as in their sequence patterns [2, 3].

Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions, including cell-cell recognition, cell-surface receptors, muscle structure and the immune system [4].

This entry represents the V-set domains, which are Ig-like domains resembling the antibody variable domain. V-set domains are found in diverse protein families, including immunoglobulin light and heavy chains; in several T-cell receptors such as CD2 (Cluster of Differentiation 2), CD4, CD80, and CD86; in myelin membrane adhesion molecules; in junction adhesion molecules (JAM); in tyrosine-protein kinase receptors; and in the programmed cell death protein 1 (PD1).

Structural links Help

PDB - click here

SCOP: b.1.1.1 , b.1.1.2 , b.1.1.4

CATH: 2.60.40.10

Database links Help

PANDIT: PF07686

Blocks: IPB013106

Pfam Clan: CL0011.22

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR013106

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O00241 Signal-regulatory protein beta-1

O88792 Junctional adhesion molecule A

P03228 33 kDa early protein

P16620 Tyrosine-protein phosphatase 69D

Q06561 Basement membrane proteoglycan

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR018031	Laminin B, subgroup
IPR001791	Laminin G
IPR013783	Immunoglobulin-like fold
IPR002172	Low density lipoprotein-receptor, class A (cysteine-rich) repeat
IPR006210	EGF-like
IPR013098	Immunoglobulin I-set
IPR016130	Protein-tyrosine phosphatase, active site
IPR008957	Fibronectin, type III-like fold
IPR013106	Immunoglobulin V-set
IPR013032	EGF-like region, conserved site
IPR000242	Protein-tyrosine phosphatase, receptor/non-receptor type
IPR012680	Laminin G, subdomain 2
IPR003961	Fibronectin, type III
IPR007110	Immunoglobulin-like
IPR003598	Immunoglobulin subtype 2
IPR003599	Immunoglobulin subtype
IPR013320	Concanavalin A-like lectin/glucanase, subgroup
IPR003596	Immunoglobulin V-set, subgroup
IPR003597	Immunoglobulin C1-set
IPR002049	EGF-like, laminin
IPR000387	Dual-specific/protein-tyrosine phosphatase, conserved region
IPR013151	Immunoglobulin
IPR000034	Laminin B type IV
IPR000742	EGF-like, type 3
IPR008985	Concanavalin A-like lectin/glucanase
IPR006209	EGF
	ModBase
	SWISS-MODEL
	PDB Chain
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Smith DK, Xue H. Sequence profiles of immunoglobulin and immunoglobulin-like domains. J. Mol. Biol. 274 530-45 1997 [PubMed: 9417933] http://dx.doi.org/10.1006/jmbi.1997.1432
2.	Potapov V, Sobolev V, Edelman M, Kister A, Gelfand I. Protein--protein recognition: juxtaposition of domain and interface cores in immunoglobulins and other sandwich-like proteins. J. Mol. Biol. 342 665-79 2004 [PubMed: 15327963] http://dx.doi.org/10.1016/j.jmb.2004.06.072
3.	Fowler SB, Clarke J. Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state. Structure 9 355-66 2001 [PubMed: 11377196] http://dx.doi.org/10.1016/S0969-2126(01)00596-2
4.	Teichmann SA, Chothia C. Immunoglobulin superfamily proteins in Caenorhabditis elegans. J. Mol. Biol. 296 1367-83 2000 [PubMed: 10698639] http://dx.doi.org/10.1006/jmbi.1999.3497

Additional Reading Open in usermanual
	Covaceuszach S, Cassetta A, Konarev PV, Gonfloni S, Rudolph R, Svergun DI, Lamba D, Cattaneo A. Dissecting NGF interactions with TrkA and p75 receptors by structural and functional studies of an anti-NGF neutralizing antibody. J. Mol. Biol. 381 2008 881-96 [PubMed: 18635195] http://dx.doi.org/10.1016/j.jmb.2008.06.008
	Newton K, Matsumoto ML, Wertz IE, Kirkpatrick DS, Lill JR, Tan J, Dugger D, Gordon N, Sidhu SS, Fellouse FA, Komuves L, French DM, Ferrando RE, Lam C, Compaan D, Yu C, Bosanac I, Hymowitz SG, Kelley RF, Dixit VM. Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies. Cell 134 2008 668-78 [PubMed: 18724939] http://dx.doi.org/10.1016/j.cell.2008.07.039
	Lazar-Molnar E, Yan Q, Cao E, Ramagopal U, Nathenson SG, Almo SC. Crystal structure of the complex between programmed death-1 (PD-1) and its ligand PD-L2. Proc. Natl. Acad. Sci. U.S.A. 105 2008 10483-8 [PubMed: 18641123] http://dx.doi.org/10.1073/pnas.0804453105
	Farady CJ, Egea PF, Schneider EL, Darragh MR, Craik CS. Structure of an Fab-protease complex reveals a highly specific non-canonical mechanism of inhibition. J. Mol. Biol. 380 2008 351-60 [PubMed: 18514224] http://dx.doi.org/10.1016/j.jmb.2008.05.009
	Lin DY, Tanaka Y, Iwasaki M, Gittis AG, Su HP, Mikami B, Okazaki T, Honjo T, Minato N, Garboczi DN. The PD-1/PD-L1 complex resembles the antigen-binding Fv domains of antibodies and T cell receptors. Proc. Natl. Acad. Sci. U.S.A. 105 2008 3011-6 [PubMed: 18287011] http://dx.doi.org/10.1073/pnas.0712278105

InterPro 23.1