Protein Family Models

HmuY is a novel heme-binding protein [1] that recruits heme from host carriers and delivers it to its cognate outer-membrane transporter, the TonB-dependent receptor HmuR. This family of proteins is found in bacteria. Proteins in this family are typically between 214 and 278 amino acids in length. [1]. 19424422. Unique structure and stability of HmuY, a novel heme-binding. protein of Porphyromonas gingivalis.. Wojtowicz H, Guevara T, Tallant C, Olczak M, Sroka A, Potempa J,. Sola M, Olczak T, Gomis-Ruth FX;. PLoS Pathog. 2009;5:e1000419.. [2]. 17922109. Porphyromonas gingivalis HmuY and HmuR: further characterization. of a novel mechanism of heme utilization.. Olczak T, Sroka A, Potempa J, Olczak M;. Arch Microbiol. 2008;189:197-210. (from Pfam)

Date:

2024-08-14

This family includes the receptor binding domain region of the alpha-2-macroglobulin family. [1]. 10625650. NMR solution structure of the receptor binding domain of human. alpha(2)-macroglobulin.. Huang W, Dolmer K, Liao X, Gettins PG;. J Biol Chem 2000;275:1089-1094.. [2]. 11106161. Structure of a rat alpha 1-macroglobulin receptor-binding domain. dimer.. Xiao T, DeCamp DL, Spran SR;. Protein Sci 2000;9:1889-1897.. [3]. 11387479. Structure of complement receptor 2 in complex with its C3d. ligand.. Szakonyi G, Guthridge JM, Li D, Young K, Holers VM, Chen XS;. Science 2001;292:1725-1728.. [4]. 10825534. Structure at 1.44 A resolution of an N-terminally truncated form. of the rat serum complement C3d fragment.. Zanotti G, Bassetto A, Battistutta R, Folli C, Arcidiaco P,. Stoppini M, Berni R;. Biochim Biophys Acta 2000;1478:232-238.. [5]. 22290936. The crystal structure of human alpha2-macroglobulin reveals a. unique molecular cage.. Marrero A, Duquerroy S, Trapani S, Goulas T, Guevara T, Andersen. GR, Navaza J, Sottrup-Jensen L, Gomis-Ruth FX;. Angew Chem Int Ed Engl. 2012;51:3340-3344. (from Pfam)

Date:

2024-08-14

Alpha-2-macroglobulins (A2Ms) are plasma proteins that trap and inhibit a broad range of proteases and are major components of the eukaryotic innate immune system. However, A2M-like proteins were identified in pathogenically invasive bacteria and species that colonize higher eukaryotes. This domain is found in eukaryotic and bacterial proteins. In human A2Ms, this domain encompasses macroglobulin-like domain MG5 and 6 including bait region. In Salmonella enterica ser A2Ms, this domain encompasses MG7 and MG8 including the bait region [1] [2]. The Bait region is cleaved by proteases, followed by a large conformational change that blocks the target protease within a cage-like complex. This model of protease entrapment is recognised as the Venus flytrap mechanism [1]. [1]. 25221932. Structure of a bacterial alpha2-macroglobulin reveals mimicry of. eukaryotic innate immunity.. Wong SG, Dessen A;. Nat Commun. 2014;5:4917.. [2]. 22290936. The crystal structure of human alpha2-macroglobulin reveals a. unique molecular cage.. Marrero A, Duquerroy S, Trapani S, Goulas T, Guevara T, Andersen. GR, Navaza J, Sottrup-Jensen L, Gomis-Ruth FX;. Angew Chem Int Ed Engl. 2012;51:3340-3344. (from Pfam)

Date:

2024-08-14

This is the MG2 (macroglobulin) domain of alpha-2-macroglobulin in eukaryotes [1]. Alpha-2-macroglobulins (A2Ms) are plasma proteins that trap and inhibit a broad range of proteases and are major components of the eukaryotic innate immune system. However, A2M-like proteins were identified in pathogenically invasive bacteria and species that colonize higher eukaryotes. This domain is found in eukaryotic and bacterial proteins. In human A2Ms, this domain is termed macroglobulin-like (MG) domain 2 and in Salmonella enterica ser A2Ms, this is domain 4 [2] [3]. [1]. 16177781. Structures of complement component C3 provide insights into the. function and evolution of immunity.. Janssen BJ, Huizinga EG, Raaijmakers HC, Roos A, Daha MR,. Nilsson-Ekdahl K, Nilsson B, Gros P;. Nature. 2005;437:505-511.. [2]. 25221932. Structure of a bacterial alpha2-macroglobulin reveals mimicry of. eukaryotic innate immunity.. Wong SG, Dessen A;. Nat Commun. 2014;5:4917.. [3]. 22290936. The crystal structure of human alpha2-macroglobulin reveals a. unique molecular cage.. Marrero A, Duquerroy S, Trapani S, Goulas T, Guevara T, Andersen. GR, Navaza J, Sottrup-Jensen L, Gomis-Ruth FX;. Angew Chem Int Ed Engl. 2012;51:3340-3344. (from Pfam)

Date:

2024-08-14

An extracellular domain found in many receptors [1]. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerisation of the phosphatase ectoprotein and in cell adhesion [2,3]. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases [4]. [1]. 8387703. An adhesive domain detected in functionally diverse receptors.. Beckmann G, Bork P;. Trends Biochem Sci. 1993;18:40-41.. [2]. 17761881. Structure of a tyrosine phosphatase adhesive interaction reveals. a spacer-clamp mechanism.. Aricescu AR, Siebold C, Choudhuri K, Chang VT, Lu W, Davis SJ,. van der Merwe PA, Jones EY;. Science. 2007;317:1217-1220.. [3]. 16456543. Molecular analysis of receptor protein tyrosine phosphatase. mu-mediated cell adhesion.. Aricescu AR, Hon WC, Siebold C, Lu W, van der Merwe PA, Jones. EY;. EMBO J. 2006;25:701-712.. [4]. 22988105. Structural basis for the sheddase function of human meprin beta. metalloproteinase at the plasma membrane.. Arolas JL, Broder C, Jefferson T, Guevara T, Sterchi EE, Bode W,. Stocker W, Becker-Pauly C, Gomis-Ruth FX;. Proc Natl Acad Sci U S A. 2012;109:16131-16136. (from Pfam)

Date:

2024-08-14