Helix-loop-helix motif in GnRH associated peptide is critical for negative regulation of prolactin secretion

Chavali, G.B.; Nagpal, Sushma; Majumdar, Subeer S.; Singh, Om; Salunke, Dinakar M.

doi:10.1006/jmbi.1997.1274

Cited by 21 publications

(15 citation statements)

References 44 publications

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“…1C). Notably, it was shown previously that the isolated prodomain of GnRH also shows significant ␣-helical propensity in circular dichroism spectra (51).…”

Section: ␣-Helical Domains Promote Er Importmentioning

confidence: 89%

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The α-Helical Structure of Prodomains Promotes Translocation of Intrinsically Disordered Neuropeptide Hormones into the Endoplasmic Reticulum

Dirndorfer

Seidel

Nimrod

et al. 2013

Journal of Biological Chemistry

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Background: Intrinsically disordered neuropeptide hormones are synthesized as larger precursors with an ␣-helical prodomain. Results:The prodomain promotes productive import of the hormone domain into the endoplasmic reticulum (ER) by its propensity to adopt an ␣-helical structure. Conclusion: Impaired ER import of intrinsically disordered proteins can be restored by ␣-helical prodomains. Significance: Secondary structure of the nascent chain can regulate translocation into the ER.

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“…1C). Notably, it was shown previously that the isolated prodomain of GnRH also shows significant ␣-helical propensity in circular dichroism spectra (51).…”

Section: ␣-Helical Domains Promote Er Importmentioning

confidence: 89%

“…For example, the prodomain of somatostatin itself comprises another peptide hormone named neuronostatin, which regulates different neuronal functions (66). Similarly, part of the prodomain of GnRH known as GnRHassociated peptide is present in GnRH-containing secretory granules and inhibits prolactin secretion (51).…”

Section: Journal Of Biological Chemistrymentioning

confidence: 99%

The α-Helical Structure of Prodomains Promotes Translocation of Intrinsically Disordered Neuropeptide Hormones into the Endoplasmic Reticulum

Dirndorfer

Seidel

Nimrod

et al. 2013

Journal of Biological Chemistry

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“…It is not uncommon, however, that completely unrelated molecules share common receptors, possibly through similar structural and/or chemical features involved in recognition and binding, resulting in molecular mimicry (1)(2)(3). Molecular mimicry often occurs by design and manifests as a control during various regulatory mechanisms (4).…”

mentioning

confidence: 99%

Structural Evaluation of a Mimicry-Recognizing Paratope: Plasticity in Antigen–Antibody Interactions Manifests in Molecular Mimicry

Tapryal

Gaur

Kaur

et al. 2013

The Journal of Immunology

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Molecular mimicry manifests antagonistically with respect to the specificity of immune recognition. However, it often occurs because different Ags share surface topologies in terms of shape or chemical nature. It also occurs when a flexible paratope accommodates dissimilar Ags by adjusting structural features according to the antigenic epitopes or differential positioning in the Ag combining site. Toward deciphering the structural basis of molecular mimicry, mAb 2D10 was isolated from a maturing immune response elicited against methyl α-d-mannopyranoside and also bound equivalently to a dodecapeptide. The physicochemical evidence of this carbohydrate–peptide mimicry in the case of mAb 2D10 had been established earlier. These studies had strongly suggested direct involvement of a flexible paratope in the observed mimicry. Surprisingly, comparison of the Ag-free structure of single-chain variable fragment 2D10 with those bound to sugar and peptide Ags revealed a conformationally invariant state of the Ab while binding to chemically and structurally disparate Ags. This equivalent binding of the two dissimilar Ags was through mutually independent interactions, demonstrating functional equivalence in the absence of structural correlation. Thus, existence of a multispecific, mature Ab in the secondary immune response was evident, as was the plasticity in the interactions while accommodating topologically diverse Ags. Although our data highlight the structural basis of receptor multispecificity, they also illustrate mechanisms adopted by the immune system to neutralize the escape mutants generated during pathogenic insult.

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“…In molecular mimicry, however, the specificity is obviously violated by completely unrelated molecules exhibiting functional equivalence. The functional mimicry involving unrelated molecules is often used as an effective control during various regulatory mechanisms (1,2). However, sometimes the accidental structural similarities lead to aberrations such as autoimmune disorders (3,4).…”

mentioning

confidence: 99%

“…Concanavalin A (ConA), 1 a lectin from Canavalia ensiformis, has been exploited for addressing the structural basis of molecular mimicry (10 -13). The mannose-containing carbohydrates on the cell surface have been characterized to be the specific ligands of ConA (14).…”

mentioning

confidence: 99%

Functional Equality in the Absence of Structural Similarity

Goel¹,

Jain²,

Kaur³

et al. 2001

Journal of Biological Chemistry

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Helix-loop-helix motif in GnRH associated peptide is critical for negative regulation of prolactin secretion

Cited by 21 publications

References 44 publications

The α-Helical Structure of Prodomains Promotes Translocation of Intrinsically Disordered Neuropeptide Hormones into the Endoplasmic Reticulum

The α-Helical Structure of Prodomains Promotes Translocation of Intrinsically Disordered Neuropeptide Hormones into the Endoplasmic Reticulum

Structural Evaluation of a Mimicry-Recognizing Paratope: Plasticity in Antigen–Antibody Interactions Manifests in Molecular Mimicry

Functional Equality in the Absence of Structural Similarity

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